Continued from EC 4.3.1 to EC 4.3.99
EC 4.4 Carbon-Sulfur Lyases
EC 4.5 Carbon-Halide Lyases
EC 4.6 Phosphorus-Oxygen Lyases
EC 4.99 Other Lyases
Accepted name: cystathionine γ-lyase
Reaction: L-cystathionine + H2O = L-cysteine + NH3 + 2-oxobutanoate (overall reaction)
(1a) L-cystathionine = L-cysteine + 2-ammoniobut-2-enoate
(1b) 2-ammoniobut-2-enoate + H2O = 2-oxobutanoate + NH3 (spontaneous)
For diagram click here.
Other name(s): homoserine deaminase; homoserine dehydratase; cystine desulfhydrase; cysteine desulfhydrase; γ-cystathionase; cystathionase; homoserine deaminase-cystathionase; γ-CTL; cystalysin; cysteine lyase; L-cystathionine cysteine-lyase (deaminating)
Systematic name: L-cystathionine cysteine-lyase (deaminating; 2-oxobutanoate-forming)
Comments: A multifunctional pyridoxal-phosphate protein. Also catalyses elimination reactions of L-homoserine to form H2O, NH3 and 2-oxobutanoate, of L-cystine, producing thiocysteine, pyruvate and NH3, and of L-cysteine producing pyruvate, NH3 and H2S.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9012-96-8
References:
1. Braunstein, A.E. and Azarkh, R.M. [Participation of vitamin B6 in enzymic formation of hydrogen sulfide from L-cysteine.] Dokl. Akad. Nauk. S.S.S.R. 71 (1950) 93-96. (in Russian)
2. Braunstein, A.E. and Azarkh, R.M. [Phosphopyridoxal in aerobic deamination of homoserine and serine.] Dokl. Akad. Nauk. S.S.S.R. 85 (1952) 385-388. (in Russian)
3. Flavin, M. and Segal, A. Purification and properties of the cystathionine γ-cleavage enzyme of Neurospora. J. Biol. Chem. 239 (1964) 2220-2227. [PMID: 14209951]
4. Matsuo, Y. and Greenberg, D.M. A crystalline enzyme that cleaves homoserine and cystathionine. III. Coenzyme resolution, activation, and inhibitors. J. Biol. Chem. 234 (1959) 507-515. [PMID: 13641250]
5. Matsuo, Y. and Greenberg, D.M. A crystalline enzyme that cleaves homoserine and cystathionine. IV. Mechanism of action, reversibility, and substrate specificity. J. Biol. Chem. 234 (1959) 516-519. [PMID: 13641251]
Accepted name: homocysteine desulfhydrase
Reaction: L-homocysteine + H2O = hydrogen sulfide + NH3 + 2-oxobutanoate (overall reaction)
(1a) L-homocysteine = hydrogen sulfide + 2-ammoniobut-2-enoate
(1b) 2-ammoniobut-2-enoate + H2O = 2-oxobutanoate + NH3 (spontaneous)
For diagram click here.
Other name(s): homocysteine desulfurase, L-homocysteine hydrogen-sulfide-lyase (deaminating)
Systematic name: L-homocysteine hydrogen-sulfide-lyase (deaminating; 2-oxobutanoate-forming)
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9024-41-3
References:
1. Kallio, R.E. Function of pyridoxal phosphate in desulfhydrase systems of Proteus morganii. J. Biol. Chem. 192 (1951) 371-377. [PMID: 14917685]
Accepted name: dimethylpropiothetin dethiomethylase
Reaction: S,S-dimethyl-β-propiothetin = dimethyl sulfide + acrylate
Other name(s): desulfhydrase; S,S-dimethyl-β-propiothetin dimethyl-sulfide-lyase
Systematic name: S,S-dimethyl-β-propiothetin dimethyl-sulfide-lyase (acrylate-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9026-85-1
References:
1. Cantoni, G.L. and Anderson, D.G. Enzymatic cleavage of dimethylpropiothetin by Polysiphonia lanosa. J. Biol. Chem. 222 (1956) 171-177. [PMID: 13366990]
Accepted name: alliin lyase
Reaction: an S-alkyl-L-cysteine S-oxide = an alkyl sulfenate + 2-aminoacrylate
Other name(s): alliinase; cysteine sulfoxide lyase; alkylcysteine sulfoxide lyase; S-alkylcysteine sulfoxide lyase; L-cysteine sulfoxide lyase; S-alkyl-L-cysteine sulfoxide lyase; alliin alkyl-sulfenate-lyase
Systematic name: S-alkyl-L-cysteine S-oxide alkyl-sulfenate-lyase (2-aminoacrylate-forming)
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9031-77-0
References:
1. Durbin, R.D. and Uchytil, T.F. Purification and properties of alliin lyase from the fungus Penicillium corymbiferum. Biochim. Biophys. Acta 235 (1971) 518-520.
2. Goryachenkova, E.V. [Enzyme in garlic which forms allycine (allyinase), a protein with phosphopyridoxal.] Dokl. Akad. Nauk. S.S.S.R. 87 (1952) 457-460. (in Russian)
3. Jacobsen, J.V., Yamaguchi, M., Howard, F.D. and Bernhard, R.A. Product inhibition of the cysteine sulfoxide lyase of Tulbaghia violacea. Arch. Biochem. Biophys. 127 (1968) 252-258.
Accepted name: lactoylglutathione lyase
Reaction: (R)-S-lactoylglutathione = glutathione + methylglyoxal
Glossary: methylglyoxal = 2-oxopropanal
Other name(s): methylglyoxalase; aldoketomutase; ketone-aldehyde mutase; glyoxylase I; (R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing)
Systematic name: (R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing; glutathione-forming)
Comments: Also acts on 3-phosphoglycerol-glutathione.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9033-12-9
References:
1. Ekwall, K. and Mannervik, B. The stereochemical configuration of the lactoyl group of S-lactoylglutathionine formed by the action of glyoxalase I from porcine erythrocytes and yeast. Biochim. Biophys. Acta 297 (1973) 297-299. [PMID: 4574550]
2. Racker, E. The mechanism of action of glyoxalase. J. Biol. Chem. 190 (1951) 685-696. [PMID: 14841219]
Accepted name: S-alkylcysteine lyase
Reaction: an S-alkyl-L-cysteine + H2O = an alkyl thiol + NH3 + pyruvate
Other name(s): S-alkylcysteinase; alkylcysteine lyase; S-alkyl-L-cysteine sulfoxide lyase; S-alkyl-L-cysteine lyase; S-alkyl-L-cysteinase; alkyl cysteine lyase; S-alkyl-L-cysteine alkylthiol-lyase (deaminating)
Systematic name: S-alkyl-L-cysteine alkyl-thiol-lyase (deaminating; pyruvate-forming)
Comments: A pyridoxal-phosphate protein. Decomposes S-alkyl-L-cysteines by α,β-elimination. Possibly identical, in yeast, with EC 4.4.1.8 cystathionine β-lyase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 62213-27-8
References:
1. Nomura, J., Nishizuka, Y. and Hayaishi, O. S-Alkylcysteinase: enzymatic cleavage of S-methyl-L-cysteine and its sulfoxide. J. Biol. Chem. 238 (1963) 1441-1446.
[EC 4.4.1.7 Deleted entry: S-(hydroxyalkyl)glutathione lyase. Now included with EC 2.5.1.18 glutathione transferase (EC 4.4.1.7 created 1972, deleted 1976)]
Accepted name: cystathionine β-lyase
Reaction: L-cystathionine + H2O = L-homocysteine + NH3 + pyruvate
Other name(s): β-cystathionase; cystine lyase; cystathionine L-homocysteine-lyase (deaminating); L-cystathionine L-homocysteine-lyase (deaminating)
Systematic name: L-cystathionine L-homocysteine-lyase (deaminating; pyruvate-forming)
Comments: A pyridoxal-phosphate protein. The enzyme from some sources also acts on L-cystine, forming pyruvate, ammonia and cysteine persulfide, and a number of related compounds. Possibly identical, in yeast, with EC 4.4.1.6 S-alkylcysteine lyase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9055-05-4
References:
1. Anderson, N.W. and Thompson, J.F. Cystine lyase: β-cystathionase from turnip roots. Phytochemistry 18 (1979) 1953-1958.
2. Flavin, M. and Slaughter, C. Cystathionine cleavage enzymes of Neurospora. J. Biol. Chem. 239 (1964) 2212-2219. [PMID: 14209950]
Accepted name: L-3-cyanoalanine synthase
Reaction: L-cysteine + hydrogen cyanide = hydrogen sulfide + L-3-cyanoalanine
Other name(s): β-cyanoalanine synthase; β-cyanoalanine synthetase; β-cyano-L-alanine synthase; L-cysteine hydrogen-sulfide-lyase (adding HCN)
Systematic name: L-cysteine hydrogen-sulfide-lyase (adding hydrogen cyanide; L-3-cyanoalanine-forming)
Comments: Contains pyridoxal phospate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9059-53-4
References:
1. Akopyan, T.N., Braunstein, A.E. and Goryachenkova, E.V. β-Cyanoalanine synthase: purification and characterization. Proc. Natl. Acad. Sci. USA 72 (1975) 1617-1621. [PMID: 1055433]
2. Castric, P.A. and Conn, E.E. Formation of β-cyanoalanine by O-acetylserine sulfhydrylase. J. Bacteriol. 108 (1971) 132-136. [PMID: 5001194]
3. Hendrickson, H.R. The β-cyanoalanine synthase of blue lupine. Fed. Proc. 27 (1968) 593 only.
4. Hendrickson, H.R. and Conn, E.E. Cyanide metabolism in higher plants. IV. Purification and properties of the β-cyanoalanine synthase of blue lupine. J. Biol. Chem. 244 (1969) 2632-2640. [PMID: 5769995]
Accepted name: cysteine lyase
Reaction: L-cysteine + sulfite = L-cysteate + hydrogen sulfide
For diagram click here.
Other name(s): cysteine (sulfite) lyase; L-cysteine hydrogen-sulfide-lyase (adding sulfite)
Systematic name: L-cysteine hydrogen-sulfide-lyase (adding sulfite; L-cysteate-forming)
Comments: A pyridoxal-phosphate protein. Can use a second molecule of cysteine (producing lanthionine), or other alkyl thiols, as a replacing agent.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9079-86-1
References:
1. Tolosa, E.A., Chepurnova, N.K., Khomutov, R.M. and Severin, E.S. Reactions catalysed by cysteine lyase from the yolk sac of chicken embryo. Biochim. Biophys. Acta 171 (1969) 369-371. [PMID: 5813025]
Accepted name: methionine γ-lyase
Reaction: L-methionine + H2O = methanethiol + NH3 + 2-oxobutanoate (overall reaction)
(1a) L-methionine = methanethiol + 2-ammoniobut-2-enoate
(1b) 2-ammoniobut-2-enoate + H2O = 2-oxobutanoate + NH3 (spontaneous)
For diagram click here.
Other name(s): L-methioninase; methionine lyase; methioninase; methionine dethiomethylase; L-methionine γ-lyase; L-methionine methanethiol-lyase (deaminating)
Systematic name: L-methionine methanethiol-lyase (deaminating; 2-oxobutanoate-forming)
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, UM-BBD, Metacyc, PDB, UM-BBD, CAS registry number: 42616-25-1
References:
1. Kreis, W. and Hession, C. Isolation and purification of L-methionine-α-deamino-γ-mercaptomethane-lyase (L-methioninase) from Clostridium sporogenes. Cancer Res. 33 (1973) 1862-1865. [PMID: 4720797]
[EC 4.4.1.12 Deleted entry: sulfoacetaldehyde lyase. Activity due to EC 2.3.3.15, sulfoacetaldehyde acetyltransferase. (EC 4.4.1.12 created 1976, deleted 2003)]
Accepted name: cysteine-S-conjugate β-lyase
Reaction: RS-CH2-CH(NH3+)COO- + H2O = RSH + NH3 + pyruvate
Other name(s): cysteine conjugate β-lyase; glutamine transaminase K/cysteine conjugate β-lyase; L-cysteine-S-conjugate thiol-lyase (deaminating)
Systematic name: L-cysteine-S-conjugate thiol-lyase (deaminating; pyruvate-forming)
Comments: A pyridoxal-phosphate protein. In the reaction, RH may represent aromatic compounds such as 4-bromobenzene and 2,4-dinitrobenzene.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 68652-57-3
References:
1. Tateishi, M., Suzuki, S. and Shimizu, H. Cysteine conjugate β-lyase in rat liver. A novel enzyme catalyzing formation of thiol-containing metabolites of drugs. J. Biol. Chem. 253 (1978) 8854-8859. [PMID: 721818]
Accepted name: 1-aminocyclopropane-1-carboxylate synthase
Reaction: S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + methylthioadenosine
For diagram of reaction click here.
Other name(s): 1-aminocyclopropanecarboxylate synthase; 1-aminocyclopropane-1-carboxylic acid synthase; 1-aminocyclopropane-1-carboxylate synthetase; aminocyclopropanecarboxylic acid synthase; aminocyclopropanecarboxylate synthase; ACC synthase; S-adenosyl-L-methionine methylthioadenosine-lyase
Systematic name: S-adenosyl-L-methionine methylthioadenosine-lyase (1-aminocyclopropane-1-carboxylate-forming)
Comments: A pyridoxal-phosphate protein. The enzyme catalyses an α,γ-elimination.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 72506-68-4
References:
1. Boller, T., Herner, R.C. and Kende, H. Assay for and enzymatic formation of an ethylene precursor, 1-aminocyclopropane-1-carboxylic acid. Planta 145 (1979) 293-303.
2. Yu, Y.-B., Adams, D.O. and Yang, S.F. 1-Aminocyclopropanecarboxylate synthase, a key enzyme in ethylene biosynthesis. Arch. Biochem. Biophys. 198 (1979) 280-296. [PMID: 507845]
Accepted name: D-cysteine desulfhydrase
Reaction: D-cysteine + H2O = sulfide + NH3 + pyruvate
Other name(s): D-cysteine lyase; D-cysteine sulfide-lyase (deaminating)
Systematic name: D-cysteine sulfide-lyase (deaminating; pyruvate-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 84012-74-8
References:
1. Nagasawa, T., Ishii, T., Kumagai, H. and Yamada, H. D-Cysteine desulfhydrase of Escherichia coli. Purification and characterization. Eur. J. Biochem. 153 (1985) 541-551. [PMID: 3908101]
2. Schmidt, A. A cysteine desulfhydrase from spinach leaves specific for D-cysteine. Z. Pflanzenphysiol. 107 (1982) 301-312.
3. Schmidt, A. and Erdle, I. A cysteine desulfhydrase specific for D-cysteine from the green-alga Chlorella fusca. Z. Naturforsch. C: Biosci. 38 (1983) 428-435.
Accepted name: selenocysteine lyase
Reaction: L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor
Other name(s): selenocysteine reductase; selenocysteine β-lyase
Systematic name: L-selenocysteine selenide-lyase (L-alanine-forming)
Comments: A pyridoxal-phosphate protein. Dithiothreitol or 2-mercaptoethanol can act as the reducing agent in the reaction. The enzyme does not act on cysteine, serine or chloroalanine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 82047-76-5
References:
1. Esaki, N., Nakamura, T., Tanaka, H. and Soda, K. Selenocysteine lyase, a novel enzyme that specifically acts on selenocysteine. Mammalian distribution and purification and properties of pig liver enzyme. J. Biol. Chem. 257 (1982) 4386-4391. [PMID: 6461656]
Accepted name: holocytochrome-c synthase
Reaction: holocytochrome c = apocytochrome c + heme
Other name(s): cytochrome c heme-lyase; holocytochrome c synthetase; holocytochrome-c apocytochrome-c-lyase
Systematic name: holocytochrome-c apocytochrome-c-lyase (heme-forming)
Comments: In the reverse direction, the enzyme catalyses the attachment of heme to two cysteine residues in the protein, forming thioether links.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 75139-03-6
References:
1. Dumont, M.E., Ernst, J.F., Hampsey, D.M. and Sherman, F. Identification and sequence of the gene encoding cytochrome c heme lyase in the yeast Saccharomyces cerevisiae. EMBO J. 6 (1987) 235-241. [PMID: 3034577]
[EC 4.4.1.18 Transferred entry: now EC 1.8.3.5, prenylcysteine lyase (EC 4.4.1.18 created 2000, deleted 2002)]
Accepted name: phosphosulfolactate synthase
Reaction: (2R)-2-O-phospho-3-sulfolactate = phosphoenolpyruvate + bisulfite
For diagram of reaction click here (mechanism)
Other name(s): (2R)-phospho-3-sulfolactate synthase; (2R)-O-phospho-3-sulfolactate sulfo-lyase
Systematic name: (2R)-2-O-phospho-3-sulfolactate hydrogen-sulfite-lyase (phosphoenolpyruvate-forming)
Comments: Requires Mg2+. The enzyme from Methanococcus jannaschii catalyses the Michael addition of sulfite to phosphoenolpyruvate. It specifically requires phosphoenolpyruvate and its broad alkaline pH optimum suggests that it uses sulfite rather than bisulfite.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 473575-53-0
References:
1. Graham, D.E., Xu, H. and White, R.H. Identification of coenzyme M biosynthetic phosphosulfolactate synthase: a new family of sulfonate-biosynthesizing enzymes. J. Biol. Chem. 277 (2002) 13421-13429. [PMID: 11830598]
Accepted name: leukotriene-C4 synthase
Reaction: leukotriene C4 = leukotriene A4 + glutathione
For diagram click here.
Other name(s): leukotriene C4 synthetase; LTC4 synthase; LTC4 synthetase; leukotriene A4:glutathione S-leukotrienyltransferase; (7E,9E,11Z,14Z)-(5S,6R)-5,6-epoxyicosa-7,9,11,14-tetraenoate:glutathione leukotriene-transferase (epoxide-ring-opening); (7E,9E,11Z,14Z)-(5S,6R)-6-(glutathion-S-yl)-5-hydroxyicosa-7,9,11,14-tetraenoate glutathione-lyase (epoxide-forming)
Systematic name: leukotriene-C4 glutathione-lyase (leukotriene-A4-forming)
Comments: The reaction proceeds in the direction of addition. Not identical with EC 2.5.1.18, glutathione transferase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 90698-32-1
References:
1. Bach, M.K., Brashler, J.R. and Morton, D.R., Jr. Solubilization and characterization of the leukotriene C4 synthetase of rat basophil leukemia cells: a novel, particulate glutathione S-transferase. Arch. Biochem. Biophys. 230 (1984) 455-465. [PMID: 6324687]
2. Shimizu, T. Enzymes functional in the syntheses of leukotrienes and related compounds. Int. J. Biochem. 20 (1988) 661-666. [PMID: 2846379]
3. Lam, B.K. and Austen, K.F. Leukotriene C4 synthase: a pivotal enzyme in cellular biosynthesis of the cysteinyl leukotrienes. Prostaglandins Other Lipid Mediat. 68-69 (2002) 511-520. [PMID: 12432940]
4. Christmas, P., Weber, B.M., McKee, M., Brown, D. and Soberman, R.J. Membrane localization and topology of leukotriene C4 synthase. J. Biol. Chem. 277 (2002) 28902-28908. [PMID: 12023288]
Accepted name: S-ribosylhomocysteine lyase
Reaction: S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione
For diagram click here.
Other name(s): S-ribosylhomocysteinase; LuxS
Systematic name: S-(5-deoxy-D-ribos-5-yl)-L-homocysteine L-homocysteine-lyase [(4S)-4,5-dihydroxypentan-2,3-dione-forming]
Comments: Contains Fe2+. The 4,5-dihydroxypentan-2,3-dione formed spontaneously cyclizes and combines with borate to form an autoinducer (AI-2) in the bacterial quorum-sensing mechanism, which is used by many bacteria to control gene expression in response to cell density [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37288-63-4
References:
1. Zhu, J., Dizin, E., Hu, X., Wavbreille, A.S., Park, J. and Pei, D. S-Ribosylhomocysteinase (LuxS) is a mononuclear iron protein. Biochemistry 42 (2003) 4717-4726. [PMID: 12705835]
2. Miller, M.B. and Bassler, B.L. Quorum sensing in bacteria. Annu. Rev. Microbiol. 55 (2001) 165-199. [PMID: 11544353]
Accepted name: S-(hydroxymethyl)glutathione synthase
Reaction: S-(hydroxymethyl)glutathione = glutathione + formaldehyde
Other name(s): glutathione-dependent formaldehyde-activating enzyme; Gfa; S-(hydroxymethyl)glutathione formaldehyde-lyase
Systematic name: S-(hydroxymethyl)glutathione formaldehyde-lyase (glutathione-forming)
Comments: The enzyme from Paracoccus denitrificans accelerates the spontaneous reaction in which the adduct of formaldehyde and glutathione is formed, i.e. the substrate for EC 1.1.1.284, S-(hydroxymethyl)glutathione dehydrogenase, in the formaldehyde-detoxification pathway.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 425642-27-9
References:
1. Goenrich, M., Bartoschek, S., Hagemeier, C.H., Griesinger, C. and Vorholt, J.A. A glutathione-dependent formaldehyde-activating enzyme (Gfa) from Paracoccus denitrificans detected and purified via two-dimensional proton exchange NMR spectroscopy. J. Biol. Chem. 277 (2002) 3069-3072. [PMID: 11741920]
Accepted name: 2-hydroxypropyl-CoM lyase
Reaction: (1) (R)-2-hydroxypropyl-CoM = (R)-1,2-epoxypropane + HS-CoM
(2) (S)-2-hydroxypropyl-CoM = (S)-1,2-epoxypropane + HS-CoM
For diagram click here.
Glossary:
coenzyme M (CoM) = 2-mercaptoethanesulfonate
Other name(s): epoxyalkane:coenzyme M transferase; epoxyalkane:CoM transferase; epoxyalkane:2-mercaptoethanesulfonate transferase; coenzyme M-epoxyalkane ligase; epoxyalkyl:CoM transferase; epoxypropane:coenzyme M transferase; epoxypropyl:CoM transferase; EaCoMT; 2-hydroxypropyl-CoM:2-mercaptoethanesulfonate lyase (epoxyalkane-ring-forming); (R)-[or (S)-]2-hydroxypropyl-CoM:2-mercaptoethanesulfonate lyase (epoxyalkane-ring-forming)
Systematic name: (R)-2-hydroxypropyl-CoM:2-mercaptoethanesulfonate lyase (cyclizing; (R)-1,2-epoxypropane-forming)
Comments: Requires zinc. Acts on both enantiomers of chiral epoxyalkanes to form the corresponding (R)- and (S)-2-hydroxyalkyl-CoM adducts. The enzyme will function with some other thiols (e.g., 2-sulfanylethanol) as the nucleophile. Uses short-chain epoxyalkanes from C2 (epoxyethane) to C6 (1,2-epoxyhexane). This enzyme forms component I of a four-component enzyme system {comprising EC 4.4.1.23 (2-hydroxypropyl-CoM lyase; component I), EC 1.8.1.5 [2-oxopropyl-CoM reductase (carboxylating); component II], EC 1.1.1.268 [2-(R)-hydroxypropyl-CoM dehydrogenase; component III] and EC 1.1.1.269 [2-(S)-hydroxypropyl-CoM dehydrogenase; component IV]} that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 244301-07-3
References:
1. Allen, J.R., Clark, D.D., Krum, J.G. and Ensign, S.A. A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial pathway of aliphatic epoxide carboxylation. Proc. Natl. Acad. Sci. USA 96 (1999) 8432-8437. [PMID: 10411892]
2. Krum, J.G., Ellsworth, H., Sargeant, R.R., Rich, G. and Ensign, S.A. Kinetic and microcalorimetric analysis of substrate and cofactor interactions in epoxyalkane:CoM transferase, a zinc-dependent epoxidase. Biochemistry 41 (2002) 5005-5014. [PMID: 11939797]
3. Coleman, N.V. and Spain, J.C. Epoxyalkane: coenzyme M transferase in the ethene and vinyl chloride biodegradation pathways of Mycobacterium strain JS60. J. Bacteriol. 185 (2003) 5536-5545. [PMID: 12949106]
Accepted name: (2R)-sulfolactate sulfo-lyase
Reaction: (2R)-3-sulfolactate = pyruvate + bisulfite
Other name(s): Suy; SuyAB; 3-sulfolactate bisulfite-lyase; sulfolactate sulfo-lyase (ambigious)
Systematic name: (2R)-3-sulfolactate bisulfite-lyase (pyruvate-forming)
Comments: Requires iron(II). This inducible enzyme participates in cysteate degradation in Paracoccus pantotrophus NKNCYSA and in 3-sulfolactate degradation in Chromohalobacter salexigens. The enzyme is specific for the (R) isomer.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 1256650-35-7
References:
1. Graham, D.E. and White, R.H. Elucidation of methanogenic coenzyme biosyntheses: from spectroscopy to genomics. Nat. Prod. Rep. 19 (2002) 133-147. [PMID: 12013276]
2. Rein, U., Gueta, R., Denger, K., Ruff, J., Hollemeyer, K. and Cook, A.M. Dissimilation of cysteate via 3-sulfolactate sulfo-lyase and a sulfate exporter in Paracoccus pantotrophus NKNCYSA. Microbiology 151 (2005) 737-747. [PMID: 15758220]
3. Denger, K. and Cook, A.M. Racemase activity effected by two dehydrogenases in sulfolactate degradation by Chromohalobacter salexigens: purification of (S)-sulfolactate dehydrogenase. Microbiology 156 (2010) 967-974. [PMID: 20007648]
Accepted name: L-cysteate sulfo-lyase
Reaction: L-cysteate + H2O = pyruvate + bisulfite + NH3
Glossary: L-cysteate = (2S)-2-amino-3-sulfopropanoate
Other name(s): L-cysteate sulfo-lyase (deaminating); CuyA
Systematic name: L-cysteate bisulfite-lyase (deaminating; pyruvate-forming)
Comments: A pyridoxal-phosphate protein. D-Cysteine can also act as a substrate, but more slowly. It is converted into pyruvate, sulfide and NH3. This inducible enzyme from the marine bacterium Silicibacter pomeroyi DSS-3 forms part of the cysteate-degradation pathway.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Denger, K., Smits, T.H. and Cook, A.M. L-cysteate sulpho-lyase, a widespread, pyridoxal 5'-phosphate-coupled desulphonative enzyme purified from Silicibacter pomeroyi DSS-3 T. Biochem. J. 394 (2005) 657-664. [PMID: 16302849]
Accepted name: olivetolic acid cyclase
Reaction: 3,5,7-trioxododecanoyl-CoA = CoA + 2,4-dihydroxy-6-pentylbenzoate
For diagram of reaction click here.
Glossary: 2,4-dihydroxy-6-pentylbenzoate = olivetolate
Other name(s): OAC
Systematic name: 3,5,7-trioxododecanoyl-CoA CoA-lyase (olivetolate-forming)
Comments: Part of the cannabinoids biosynthetic pathway in the plant Cannabis sativa.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Gagne, S.J., Stout, J.M., Liu, E., Boubakir, Z., Clark, S.M. and Page, J.E. Identification of olivetolic acid cyclase from Cannabis sativa reveals a unique catalytic route to plant polyketides. Proc. Natl. Acad. Sci. USA 109 (2012) 12811-12816. [PMID: 22802619]
Accepted name: DDT-dehydrochlorinase
Reaction: 1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane = 1,1-dichloro-2,2-bis(4-chlorophenyl)ethylene + chloride
Other name(s): DDT-as; 1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane chloride-lyase
Systematic name: 1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane chloride-lyase [1,1-dichloro-2,2-bis(4-chlorophenyl)ethylene-forming]
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 9031-20-3
References:
1. Lipke, H. and Kearns, C.W. DDT dechlorinase. I. Isolation, chemical properties, and spectrophotometric assay. J. Biol. Chem. 234 (1959) 2123-2128. [PMID: 13673024]
2. Lipke, H. and Kearns, C.W. DDT dechlorinase. II. Substrate and cofactor specificity. J. Biol. Chem. 234 (1959) 2129-2132. [PMID: 13673025]
3. Moorefield, H.H. Purification of DDT-dehydrochlorinase from resistant houseflies. Contr. Boyce Thompson Inst. 18 (1956) 303-310.
Accepted name: 3-chloro-D-alanine dehydrochlorinase
Reaction: 3-chloro-D-alanine + H2O = pyruvate + chloride + NH3
Other name(s): β-chloro-D-alanine dehydrochlorinase; 3-chloro-D-alanine chloride-lyase (deaminating)
Systematic name: 3-chloro-D-alanine chloride-lyase (deaminating; pyruvate-forming)
Comments: A pyridoxal-phosphate protein. Also catalyses β-replacement reactions, e.g. converts 3-chloro-D-alanine and H2S into D-cysteine and HCl.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 78990-65-5
References:
1. Nagasawa, T., Ishii, T. and Yamada, H. Physiological comparison of D-cysteine desulfhydrase of Escherichia coli with 3-chloro-D-alanine dehydrochlorinase of Pseudomonas putida CR 1-1. Arch. Microbiol. 149 (1988) 413-416. [PMID: 3132906]
2. Yamada, H., Nagasawa, T., Ohkishi, H., Kawakami, B. and Tani, Y. Synthesis of D-cysteine from 3-chloro-D-alanine and hydrogen sulfide by 3-chloro-D-alanine hydrogen chloride-lyase (deaminating) of Pseudomonas putida. Biochem. Biophys. Res. Commun. 100 (1981) 1104-1110. [PMID: 6791643]
Accepted name: dichloromethane dehalogenase
Reaction: dichloromethane + H2O = formaldehyde + 2 chloride
Other name(s): dichloromethane chloride-lyase (chloride-hydrolysing); dichloromethane chloride-lyase (chloride-hydrolysing; formaldehyde-forming)
Systematic name: dichloromethane chloride-lyase (adding H2O; chloride-hydrolysing; formaldehyde-forming)
Comments: Requires glutathione.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 97002-70-5
References:
1. Kohler-Staub, D. and Leisinger, T. Dichloromethane dehalogenase of Hyphomicrobium sp. strain DM2. J. Bacteriol. 162 (1985) 676-681. [PMID: 3988708]
Accepted name: L-2-amino-4-chloropent-4-enoate dehydrochlorinase
Reaction: L-2-amino-4-chloropent-4-enoate + H2O = 2-oxopent-4-enoate + chloride + NH3
Other name(s): L-2-amino-4-chloro-4-pentenoate dehalogenase; L-2-amino-4-chloropent-4-enoate chloride-lyase (deaminating); L-2-amino-4-chloropent-4-enoate chloride-lyase (deaminating; 2-oxopent-4-enoate-forming)
Systematic name: L-2-amino-4-chloropent-4-enoate chloride-lyase (adding water; deaminating; 2-oxopent-4-enoate-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 113066-37-8
References:
1. Moriguchi, M., Hoshino, S. and Hatanaka, S.-I. Dehalogenation and deamination of l-2-amino-4-chloro-4-pentenoic acid by Proteus mirabilis. Agric. Biol. Chem. 51 (1987) 3295.
Accepted name: S-carboxymethylcysteine synthase
Reaction: 3-chloro-L-alanine + thioglycolate = S-carboxymethyl-L-cysteine + chloride
Other name(s): S-carboxymethyl-L-cysteine synthase
Systematic name: 3-chloro-L-alanine chloride-lyase (adding thioglycolate; S-carboxymethyl-L-cysteine-forming)
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 124671-39-2
References:
1. Kumagai, H., Suzuki, H., Shigematsu, H. and Tuchikura, T. S-Carboxymethylcysteine synthase from Escherichia coli. Agric. Biol. Chem. 53 (1989) 2481-2487.
Accepted name: adenylate cyclase
Reaction: ATP = 3',5'-cyclic AMP + diphosphate
Other name(s): adenylylcyclase; adenyl cyclase; 3',5'-cyclic AMP synthetase; ATP diphosphate-lyase (cyclizing)
Systematic name: ATP diphosphate-lyase (cyclizing; 3',5'-cyclic-AMP-forming)
Comments: Also acts on dATP to form 3',5'-cyclic dAMP. Requires pyruvate. Activated by NAD+ in the presence of EC 2.4.2.31 NAD(P)+—arginine ADP-ribosyltransferase.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9012-42-4
References:
1. Hirata, M. and Hayaishi, O. Adenyl cyclase of Brevibacterium liquefaciens. Biochim. Biophys Acta 149 (1967) 1-11. [PMID: 4295782]
Accepted name: guanylate cyclase
Reaction: GTP = 3',5'-cyclic GMP + diphosphate
For diagram of reaction click here
Other name(s): guanylyl cyclase; guanyl cyclase; GTP diphosphate-lyase (cyclizing)
Systematic name: GTP diphosphate-lyase (cyclizing; 3',5'-cyclic-GMP-forming)
Comments: Also acts on ITP and dGTP.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9054-75-5
References:
1. Garbers, D.L., Suddath, J.L. and Hardman, J.G. Enzymatic formation of inosine 3',5'-monophosphate and of 2'-deoxyguanosine 3',5'-monophosphate. Inosinate and deoxyguanylate cyclase activity. Biochim. Biophys. Acta 377 (1975) 174-185. [PMID: 235291]
2. Hardman, J.G. and Sutherland, E.W. Guanyl cyclase, an enzyme catalyzing the formation of guanosine 3',5'-monophosphate from guanosine triphosphate. J. Biol. Chem. 244 (1969) 6363-6370. [PMID: 4982201]
[EC 4.6.1.3 Transferred entry: now EC 4.2.3.4, 3-dehydroquinate synthase (EC 4.6.1.3 created 1978, deleted 2000)]
[EC 4.6.1.4 Transferred entry: now EC 4.2.3.5, chorismate synthase (EC 4.6.1.4 created 1978, modified 1983, deleted 2000)]
[EC 4.6.1.5 Transferred entry: now EC 4.2.3.7 pentalenene synthase (EC 4.6.1.5 created 1989, deleted 2000)]
Accepted name: cytidylate cyclase
Reaction: CTP = 3',5'-cyclic CMP + diphosphate
Other name(s): 3',5'-cyclic-CMP synthase; cytidylyl cyclase; cytidyl cyclase; CTP diphosphate-lyase (cyclizing)
Systematic name: CTP diphosphate-lyase (cyclizing; 3',5'-cyclic-CMP-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 65357-82-6
References:
1. Cech, S.Y. and Ignarro, L.J. Cytidine 3',5'-monophosphate (cyclic CMP) formation by homogenates of mouse liver. Biochem. Biophys. Res. Commun. 80 (1978) 119-125. [PMID: 23778]
2. Newton, R.P., Salih, S.G., Hakeem, N.A., Kingston, E.E. and Beynon, J.H. 3',5'-Cyclic UMP, -cyclic IMP, -cyclic TMP and related enzymes in mammalian-tissues. Biochem. Soc. Trans. 13 (1985) 1134-1135.
[EC 4.6.1.7 Transferred entry: now EC 4.2.3.8, CASbene synthase (EC 4.6.1.7 created 1989, deleted 2000)]
[EC 4.6.1.8 Transferred entry: now EC 4.2.3.10, (–)-endo-fenchol synthase (EC 4.6.1.8 created 1992, deleted 2000)]
[EC 4.6.1.9 Transferred entry: now EC 4.2.3.11, sabinene-hydrate synthase (EC 4.6.1.9 created 1992, deleted 2000)]
[EC 4.6.1.10 Transferred entry: now EC 4.2.3.12, 6-pyruvoyltetrahydropterin synthase (EC 4.6.1.10 created 1999, deleted 2000)]
[EC 4.6.1.11 Transferred entry: now EC 4.2.3.13, trichodiene synthase (EC 4.6.1.11 created 1999, deleted 2000)]
Accepted name: 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Reaction: 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + CMP
For diagram click here.
Other name(s): MECDP-synthase; 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol CMP-lyase (cyclizing)
Systematic name: 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol CMP-lyase (cyclizing; 2-C-methyl-D-erythritol 2,4-cyclodiphosphate-forming)
Comments: The enzyme from Escherichia coli requires Mg2+ or Mn2+. Forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis (for diagram, click here).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 287480-92-6
References:
1. Herz, S., Wungsintaweekul, J., Schuhr, C.A., Hecht, S., Lüttgen, H., Sagner, S., Fellermeier, M., Eisenreich, W., Zenk, M.H., Bacher, A. and Rohdich, F. Biosynthesis of terpenoids: YgbB protein converts 4-diphosphocytidyl-2C-methyl-D-erithritol 2-phosphate to 2-C-methyl-D-erithritol 2,4-cyclodiphosphate. Proc. Natl. Acad. Sci. USA 97 (2000) 2486-2490. [PMID: 10694574]
2. Takagi, M., Kuzuyama, T., Kaneda, K., Watanabe, H., Dairi, T. and Seto, H. Studies on the nonmevalonate pathway: Formation of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate from 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. Tetrahedron Lett. 41 (2000) 3395-3398.
Accepted name: phosphatidylinositol diacylglycerol-lyase
Reaction: 1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
For diagram click here.
Other name(s): monophosphatidylinositol phosphodiesterase; phosphatidylinositol phospholipase C; 1-phosphatidylinositol phosphodiesterase; 1-phosphatidyl-D-myo-inositol inositolphosphohydrolase (cyclic-phosphate-forming); 1-phosphatidyl-1D-myo-inositol diacylglycerol-lyase (1,2-cyclic-phosphate-forming)
Systematic name: 1-phosphatidyl-1D-myo-inositol 1,2-diacyl-sn-glycerol-lyase (1D-myo-inositol-1,2-cyclic-phosphate-forming)
Comments: This enzyme is bacterial. Activity is also found in animals, but this activity is due to the presence of EC 3.1.4.11, phosphoinositide phospholipase C.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37288-19-0
References:
1. Allan, D. and Michell, R.H. Phosphatidylinositol cleavage catalysed by the soluble fraction from lymphocytes. Activity at pH5.5 and pH7.0. Biochem. J. 142 (1974) 591-597. [PMID: 4377210]
2. Friedel, R.O., Brown, J.D. and Durell, J. Monophosphatidyl inositol inositolphosphohydrolase in guinea-pig brain. Biochim. Biophys. Acta 144 (1967) 684-686. [PMID: 4294905]
3. Irvine, R.F. The enzymology of stimulated inositol lipid turnover. Cell Calcium 3 (1982) 295-309. [PMID: 6297738]
4. Michell, R.H. and Allan, D. Inositol cyclic phosphate as a product of phosphatidylinositol breakdown by phospholipase C (Bacillus cereus). FEBS Lett. 53 (1975) 302-304. [PMID: 236918]
5. Low, M.G. and Finean, J.B. Release of alkaline phosphatase fom membranes by a bacterial phosphatidylinositol phospholipase C. Biochem J. 167 (1977) 281-284. [PMID: 588258]
6. Henner, D.J., Yang, M., Chen, E., Helmikss, R. and Low, M.G. Sequence of the Bacillus thuringiensis phosphatidylinositol-specific phospholipase C. Nucleic Acids Res. 16 (1988) 10383 only. [PMID: 3194218]
Accepted name: glycosylphosphatidylinositol diacylglycerol-lyase
Reaction: 6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol = 6-(α-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
For diagram click here.
Other name(s): (glycosyl)phosphatidylinositol-specific phospholipase C; GPI-PLC; GPI-specific phospholipase C; VSG-lipase; glycosyl inositol phospholipid anchor-hydrolyzing enzyme; glycosylphosphatidylinositol-phospholipase C; glycosylphosphatidylinositol-specific phospholipase C; variant-surface-glycoprotein phospholipase C; 6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol diacylglycerol-lyase (1,2-cyclic-phosphate-forming)
Systematic name: 6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol 1,2-diacyl-sn-glycerol-lyase [6-(α-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate-forming]
Comments: This enzyme is also active when O-4 of the glucosamine is substituted by carrying the oligosaccharide that can link a protein to the structure. It therefore cleaves proteins from the lipid part of the glycosylphostphatidylinositol (GPI) anchors. In some cases, the long-chain acyl group at the sn-1 position of glycerol is replaced by an alkyl or alk-1-enyl group. In other cases, the diacylglycerol is replaced by ceramide (see Lip-1.4 and Lip-1.5 for definition). The only characterized enzyme with this specificity is from Trypanosoma brucei, where the acyl groups are myristoyl, but the function of the trypanosome enzyme is unknown. Substitution on O-2 of the inositol blocks action of this enzyme. It is not identical with EC 3.1.4.50, glycosylphosphatidylinositol phospholipase D.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 129070-68-4
References:
1. Hereld, D., Krakow, J.L., Bangs, J.D., Hart, G.W. and Englund, P.T. A phospholipase C from Trypanosoma brucei which selectively cleaves the glycolipid on the variant surface glycoprotein. J. Biol. Chem. 261 (1986) 13813-13819. [PMID: 3759991]
2. Carnall, N., Webb, H. and Carrington, M. Mutagenesis study of the glycosylphosphatidylinositol phospholipase C of Trypanosoma brucei. Mol. Biochem. Parasitol. 90 (1997) 423-432. [PMID: 9476790]
3. Armah, D.A. and Mensa-Wilmot, K. Tetramerization of glycosylphosphatidylinositol-specific phospholipase C from Trypanosoma brucei. J. Biol. Chem. 275 (2000) 19334-19342. [PMID: 10764777]
Accepted name: FAD-AMP lyase (cyclizing)
Reaction: FAD = AMP + riboflavin cyclic-4',5'-phosphate
Other name(s): FMN cyclase; FAD AMP-lyase (cyclic-FMN-forming)
Systematic name: FAD AMP-lyase (riboflavin-cyclic-4',5'-phosphate-forming)
Comments: Requires Mn2+ or Co2+. While FAD was the best substrate tested [2], the enzyme also splits ribonucleoside diphosphate-X compounds in which X is an acyclic or cyclic monosaccharide or derivative bearing an X-OH group that is able to attack internally the proximal phosphorus with the geometry necessary to form a P=X product; either a five-atom monocyclic phosphodiester or a cis-bicyclic phosphodiester-pyranose fusion. The reaction is strongly inhibited by ADP or ATP but is unaffected by the presence of the product, cFMN.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 208349-48-8
References:
1. Fraiz, F.J., Pinto, R.M., Costas, M.J., Avalos, M., Canales, J., Cabezas, A. and Cameselle, J.C. Enzymic formation of riboflavin 4',5'-cyclic phosphate from FAD: evidence for a specific low-Km FMN cyclase in rat liver. Biochem. J. 330 (1998) 881-888. [PMID: 9480905]
2. Cabezas, A., Pinto, R.M., Fraiz, F., Canales, J., Gonzalez-Santiago, S., and Cameselle, J.C. Purification, characterization, and substrate and inhibitor structure-activity studies of rat liver FAD-AMP lyase (cyclizing): preference for FAD and specificity for splitting ribonucleoside diphosphate-X into ribonucleotide and a five-atom cyclic phosphodiester of X, either a monocyclic compound or a cis-bicyclic phosphodiester-pyranose fusion. Biochemistry 40 (2001) 13710-13722. [PMID: 11695920]
Accepted name: α-D-ribose 1-methylphosphonate 5-phosphate C-P-lyase
Reaction: α-D-ribose 1-methylphosphonate 5-phosphate = α-D-ribose 1,2-cyclic phosphate 5-phosphate + methane
For diagram of reaction click here.
Other name(s): phnJ (gene name)
Systematic name: α-D-ribose-1-methylphosphonate-5-phosphate C-P-lyase (methane forming)
Comments: Isolated from Escherichia coli. Involves an [4Fe-4S] cluster and a S-adenosyl-L-methionine (SAM) radical.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Kamat, S.S., Williams, H.J. and Raushel, F.M. Intermediates in the transformation of phosphonates to phosphate by bacteria. Nature 480 (2011) 570-573. [PMID: 22089136]
Accepted name: ferrochelatase
Reaction: protoheme + 2 H+ = protoporphyrin + Fe2+
For diagram of reaction click here.
Other name(s): ferro-protoporphyrin chelatase; iron chelatase; heme synthetase; heme synthase; protoheme ferro-lyase
Systematic name: protoheme ferro-lyase (protoporphyrin-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9012-93-5
References:
1. Bloomer, J.R., Hill, H.D., Morton, K.O., Anderson-Burnham, L.A. and Straka, J.G. The enzyme defect in bovine protoporphyria. Studies with purified ferrochelatase. J.Biol. Chem. 262 (1987) 667-671. [PMID: 3805002]
2. Porra, R.J. and Jones, O.T.G. Studies on ferrochelatase. 1. Assay and properties of ferrochelatase from a pig-liver mitochondrial extract. Biochem. J. 87 (1963) 181-185.[PMID: 13972328]
3. Porra, R.J. and Jones, O.T.G. Studies on ferrochelatase. 2. An investigation of the role of ferrochelatase in the biosynthesis of various haem prosthetic groups. Biochem. J. 87 (1963) 186-192.[PMID: 13972329]
Accepted name: alkylmercury lyase
Reaction: an alkylmercury + H+ = an alkane + Hg2+
Other name(s): organomercury lyase; organomercurial lyase; alkylmercury mercuric-lyase
Systematic name: alkylmercury mercuric-lyase (alkane-forming)
Comments: Acts on CH3Hg+ and a number of other alkylmercury and arylmercury compounds, in the presence of cysteine or other thiols, liberating mercury as a mercaptide.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 72560-99-7
References:
1. Tezuka, T. and Tonomura, K. Purification and properties of an enzyme catalyzing the splitting of carbon-mercury linkages from mercury-resistant Pseudomonas K-62 strain. I. Splitting enzyme 1. J. Biochem. (Tokyo) 80 (1976) 79-87. [PMID: 9382]
Accepted name: sirohydrochlorin cobaltochelatase
Reaction: cobalt-sirohydrochlorin + 2 H+ = sirohydrochlorin + Co2+
For diagram click here.
Other name(s): CbiK; CbiX; CbiXS; anaerobic cobalt chelatase; cobaltochelatase [ambiguous]; sirohydrochlorin cobalt-lyase (incorrect)
Systematic name: cobalt-sirohydrochlorin cobalt-lyase (sirohydrochlorin-forming)
Comments: This enzyme is a type II chelatase, being either a monomer (CbiX) or a homodimer (CibK) and being ATP-independent. CbiK from Salmonella enterica uses precorrin-2 as the substrate to yield cobalt-precorrin-2. The enzyme contains two histidines at the active site that are thought to be involved in the deprotonation of the tetrapyrrole substrate as well as in metal binding. CbiX from Bacillus megaterium inserts cobalt at the level of sirohydrochlorin (factor-II) rather than precorrin-2.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Schubert, H.L., Raux, E., Wilson, K.S. and Warren, M.J. Common chelatase design in the branched tetrapyrrole pathways of heme and anaerobic cobalamin synthesis. Biochemistry 38 (1999) 10660-10669. [PMID: 10451360]
2. Brindley, A.A., Raux E., Leech, H.K., Schubert, H.L. and Warren, M.J. A story of chelatase evolution: Identification and characterisation of a small 13-15 kDa 'ancestral' cobaltochelatase (CbiXS) in the Archaea. J. Biol. Chem. 278 (2003) 22388-22395. [PMID: 12686546]
3. Warren, M.J., Raux, E., Schubert, H.L. and Escalante-Semerena, J.C. The biosynthesis of adenosylcobalamin (vitamin B12). Nat. Prod. Rep. 19 (2002) 390-412. [PMID: 12195810]
Accepted name: sirohydrochlorin ferrochelatase
Reaction: siroheme + 2 H+ = sirohydrochlorin + Fe2+
For diagram click here.
Other name(s): CysG; Met8P; SirB; sirohydrochlorin ferro-lyase (incorrect)
Systematic name: siroheme ferro-lyase (sirohydrochlorin-forming)
Comments: This enzyme catalyses the third of three steps leading to the formation of siroheme from uroporphyrinogen III. The first step involves the donation of two S-adenosyl-L-methionine-derived methyl groups to carbons 2 and 7 of uroporphyrinogen III to form precorrin-2 (EC 2.1.1.107, uroporphyrin-III C-methyltransferase) and the second step involves an NAD+-dependent dehydrogenation to form sirohydrochlorin from precorrin-2 (EC 1.3.1.76, precorrin-2 dehydrogenase). In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. In some bacteria, steps 1-3 are catalysed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirB being responsible for the above reaction.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Schubert, H.L., Raux, E., Brindley, A.A., Leech, H.K., Wilson, K.S., Hill, C.P. and Warren, M.J. The structure of Saccharomyces cerevisiae Met8p, a bifunctional dehydrogenase and ferrochelatase. EMBO J. 21 (2002) 2068-2075. [PMID: 11980703]
2. Warren, M.J., Raux, E., Schubert, H.L. and Escalante-Semerena, J.C. The biosynthesis of adenosylcobalamin (vitamin B12). Nat. Prod. Rep. 19 (2002) 390-412. [PMID: 12195810]
Accepted name: aliphatic aldoxime dehydratase
Reaction: an aliphatic aldoxime = an aliphatic nitrile + H2O
Other name(s): OxdA; aliphatic aldoxime hydro-lyase
Systematic name: aliphatic aldoxime hydro-lyase (aliphatic-nitrile-forming)
Comments: The enzyme from Pseudomonas chlororaphis contains Ca2+ and protoheme IX, the iron of which must be in the form Fe2+ for activity. The enzyme exhibits a strong preference for aliphatic aldoximes, such as butyraldoxime and acetaldoxime, over aromatic aldoximes, such as pyridine-2-aldoxime, which is a poor substrate. No activity was found with the aromatic aldoximes benzaldoxime and pyridine-4-aldoxime.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Oinuma, K-I., Hashimoto, Y., Konishi, K., Goda, M., Noguchi, T., Higashibata, H. and Kobayashi, M. Novel aldoxime dehydratase involved in carbon-nitrogen triple bond synthesis of Pseudomonas chlororaphis B23: Sequencing, gene expression, purification and characterization. J. Biol. Chem. 278 (2003) 29600-29608. [PMID: 12773527]
2. Xie, S.X., Kato, Y., Komeda, H., Yoshida, S. and Asano, Y. A gene cluster responsible for alkylaldoxime metabolism coexisting with nitrile hydratase and amidase in Rhodococcus globerulus A-4. Biochemistry 42 (2003) 12056-12066. [PMID: 14556637]
3. Kato, Y., Yoshida, S., Xie, S.-X. and Asano, Y. Aldoxime dehydratase co-existing with nitrile hydratase and amidase in the iron-type nitrile hydratase-producer Rhodococcus sp. N-771. J. Biosci. Bioeng. 97 (2004) 250-259. [PMID: 16233624]
Accepted name: indoleacetaldoxime dehydratase
Reaction: (indol-3-yl)acetaldehyde oxime = (indol-3-yl)acetonitrile + H2O
For reaction pathway click here.
Other name(s): indoleacetaldoxime hydro-lyase; 3-indoleacetaldoxime hydro-lyase; indole-3-acetaldoxime hydro-lyase; indole-3-acetaldehyde-oxime hydro-lyase; (indol-3-yl)acetaldehyde-oxime hydro-lyase
Systematic name: (indol-3-yl)acetaldehyde-oxime hydro-lyase [(indol-3-yl)acetonitrile-forming]
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9024-27-5
References:
1. Kumar, S.A. and Mahadevan, S. 3-Indoleacetaldoxime hydro-lyase: a pyridoxal-5'-phosphate activated enzyme. Arch. Biochem. Biophys. 103 (1963) 516-518. [PMID: 14099566]
2. Mahadevan, S. Conversion of 3-indoleacetoxime to 3-indoleacetonitrile by plants. Arch. Biochem. Biophys. 100 (1963) 557-558.
Accepted name: phenylacetaldoxime dehydratase
Reaction: (Z)-phenylacetaldehyde oxime = phenylacetonitrile + H2O
For diagram click here.
Other name(s): PAOx dehydratase; arylacetaldoxime dehydratase; OxdB; (Z)-phenylacetaldehyde-oxime hydro-lyase
Systematic name: (Z)-phenylacetaldehyde-oxime hydro-lyase (phenylacetonitrile-forming)
Comments: The enzyme from Bacillus sp. OxB-1 contains protoheme IX, the iron of which must be in the form iron(II) for activity. (Z)-Phenylacetaldoxime binds to ferric heme (the iron(III) form) via the oxygen atom whereas it binds to the active ferrous form via the nitrogen atom. In this way, the oxidation state of the heme controls the coordination stucture of the substrate—heme complex, which regulates enzyme activity [2]. The enzyme is active towards several (Z)-arylacetaldoximes and (E/Z)-alkylaldoximes as well as towards arylalkylaldoximes such as 3-phenylpropionaldoxime and 4-phenylbutyraldoxime. However, it is inactive with phenylacetaldoximes that have a substituent group at an α-site of an oxime group, for example, with (E/Z)-2-phenylpropionaldoxime and (E/Z)-mandelaldoxime. The activity of the enzyme is inhibited completely by the heavy-metal cations Cu+, Cu2+, Ag+ and Hg+ whereas Fe2+ and Sn2+ have an activatory effect.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 203210-76-8
References:
1. Kato, Y., Nakamura, K., Sakiyama, H., Mayhew, S.G. and Asano, Y. Novel heme-containing lyase, phenylacetaldoxime dehydratase from Bacillus sp. strain OxB-1: purification, characterization, and molecular cloning of the gene. Biochemistry 39 (2000) 800-809. [PMID: 10651646]
2. Kobayashi, K., Yoshioka, S., Kato, Y., Asano, Y. and Aono, S. Regulation of aldoxime dehydratase activity by redox-dependent change in the coordination structure of the aldoxime-heme complex. J. Biol. Chem. 280 (2005) 5486-5490. [PMID: 15596434]
Accepted name: heme ligase
Reaction: 2 ferriprotoporphyrin IX = β-hematin
Other name(s): heme detoxification protein; HDP; hemozoin synthase
Systematic name: Fe3+:ferriprotoporphyrin IX ligase (β-hematin-forming)
Comments: This heme detoxifying enzyme is found in Plasmodium parasites and converts toxic heme to crystalline hemozoin. These organisms lack the mammalian heme oxygenase for elimination of heme.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Jani, D., Nagarkatti, R., Beatty, W., Angel, R., Slebodnick, C., Andersen, J., Kumar, S. and Rathore, D. HDP-a novel heme detoxification protein from the malaria parasite. PLoS Pathog. 4 (2008) e1000053. [PMID: 18437218]