Continued from EC 2.6.1.51 to EC 2.6.1.101
EC 2.6.2 Amidinotransferases
EC 2.6.3 Oximinotransferases
EC 2.6.99 Transferring Other Nitrogenous Groups
[EC 2.6.2.1 Transferred entry: now EC 2.1.4.1 glycine amidinotransferase (EC 2.6.2.1 created 1961, deleted 1965)]
Accepted name: oximinotransferase
Reaction: pyruvate oxime + acetone = pyruvate + acetone oxime
Other name(s): transoximinase; oximase; pyruvate-acetone oximinotransferase; transoximase
Systematic name: pyruvate-oxime:acetone oximinotransferase
Comments: Acetaldehyde can act instead of acetone; D-glucose oxime can act instead of pyruvate oxime.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9030-49-3
References:
1. Yamafuji, K. and Eto, M. Chromatographic study of transoximase. Enzymologia 16 (1954) 247-255.
2. Yamafuji, K., Omura, H. and Miura, K. On the transoximase. Enzymologia 16 (1953) 75-80.
3. Yamafuji, K., Shimamura, M. and Omura, H. Measurement of transoximase action. Enzymologia 17 (1956) 359-362.
Accepted name: dATP(dGTP)—DNA purinetransferase
Reaction: (1) dATP + depurinated DNA = deoxyribose triphosphate + DNA
(2) dGTP + depurinated DNA = deoxyribose triphosphate + DNA
Systematic name: dATP(dGTP):depurinated-DNA purine transferase
Comments: The purine residue is transferred on to the apurinic site forming a normal glycosylic bond. dATP reacts at sites of the double-stranded depurinated DNA that lack adenine, and dGTP at sites that lack guanine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Deutsch, W.A. and Linn, S. DNA binding activity from cultured human fibroblasts that is specific for partially depurinated DNA and that inserts purines into apurinic sites. Proc. Natl. Acad. Sci. USA 76 (1979) 141-144. [PMID: 218192]
2. Livneh, Z., Elad, D. and Sperling, J. Enzymatic insertion of purine bases into depurinated DNA in vitro. Proc. Natl. Acad. Sci. USA 76 (1979) 1089-1093. [PMID: 375225]
Accepted name: pyridoxine 5'-phosphate synthase
Reaction: 1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = pyridoxine 5'-phosphate + phosphate + 2 H2O
For diagram, click here
Other name(s): pyridoxine 5-phosphate phospho lyase; PNP synthase; PdxJ
Systematic name: 1-deoxy-D-xylulose-5-phosphate:3-amino-2-oxopropyl phosphate 3-amino-2-oxopropyltransferase (phosphate-hydrolysing; cyclizing)
Comments: In Escherichia coli, the coenzyme pyridoxal 5'-phosphate is synthesized de novo by a pathway that involves EC 1.2.1.72 (erythrose-4-phosphate dehydrogenase), EC 1.1.1.290 (4-phosphoerythronate dehydrogenase), EC 2.6.1.52 (phosphoserine transaminase), EC 1.1.1.262 (4-hydroxythreonine-4-phosphate dehydrogenase), EC 2.6.99.2 (pyridoxine 5'-phosphate synthase) and EC 1.4.3.5 (with pyridoxine 5'-phosphate as substrate). 1-Deoxy-D-xylulose cannot replace 1-deoxy-D-xylulose 5-phosphate as a substrate [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 230310-47-1
References:
1. Garrido-Franco, M. Pyridoxine 5'-phosphate synthase: de novo synthesis of vitamin B6 and beyond. Biochim. Biophys. Acta 1647 (2003) 92-97. [PMID: 12686115]
2. Garrido-Franco, M., Laber, B., Huber, R. and Clausen, T. Enzyme-ligand complexes of pyridoxine 5'-phosphate synthase: implications for substrate binding and catalysis. J. Mol. Biol. 321 (2002) 601-612. [PMID: 12206776]
3. Laber, B., Maurer, W., Scharf, S., Stepusin, K. and Schmidt, F.S. Vitamin B6 biosynthesis: formation of pyridoxine 5'-phosphate from 4-(phosphohydroxy)-L-threonine and 1-deoxy-D-xylulose-5-phosphate by PdxA and PdxJ protein. FEBS Lett. 449 (1999) 45-48. [PMID: 10225425]
4. Franco, M.G., Laber, B., Huber, R. and Clausen, T. Structural basis for the function of pyridoxine 5'-phosphate synthase. Structure 9 (2001) 245-253. [PMID: 11286891]