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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 2.6.1.52

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 2.6.1.52

Enzymes and Genes:
3-phosphoserine aminotransferase Inferred from experiment : serC ( Escherichia coli K-12 substr. MG1655 )
phosphoserine aminotransferase Inferred from experiment : PSAT1 ( Homo sapiens )
phosphoserine aminotransferase Inferred from experiment : serC ( Methanosarcina acetivorans )
phosphoserine aminotransferase Inferred from experiment : serC ( Methanocaldococcus jannaschii )
phosphoserine aminotransferase Inferred from experiment : PSAT ( Arabidopsis thaliana col )
phosphoserine aminotransferase 1 Inferred from experiment : Psat1 ( Rattus norvegicus )

In Pathway: serine biosynthesis

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: Balanced.

Enzyme Commission Primary Name: phosphoserine transaminase

Enzyme Commission Synonyms: PSAT, phosphoserine aminotransferase, 3-phosphoserine aminotransferase, hydroxypyruvic phosphate-glutamic transaminase, L-phosphoserine aminotransferase, phosphohydroxypyruvate transaminase, phosphohydroxypyruvic-glutamic transaminase, 3-O-phospho-L-serine:2-oxoglutarate aminotransferase, SerC, PdxC, 3PHP transaminase

Standard Gibbs Free Energy (ΔrG in kcal/mol): 0.07583618 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
A pyridoxal-phosphate protein. This enzyme catalyses the second step in the phosphorylated pathway of serine biosynthesis in Escherichia coli [Pizer63, Zhao96]. It also catalyses the third step in the biosynthesis of the coenzyme pyridoxal 5-phosphate in Escherichia coli (using Reaction 2 above) [Zhao96]. In Escherichia coli, 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). Pyridoxal phosphate is the cofactor for both activities and therefore seems to be involved in its own biosynthesis [Drewke96]. Non-phosphorylated forms of serine and threonine are not substrates [Drewke96].

Citations: [Hirsch67, Zhao96b]

Gene-Reaction Schematic: ?

Unification Links: KEGG:R04173 , Rhea:14329

Relationship Links: BRENDA:EC:2.6.1.52 , ENZYME:EC:2.6.1.52 , IUBMB-ExplorEnz:EC:2.6.1.52 , UniProt:RELATED-TO:O34370 , UniProt:RELATED-TO:P10658 , UniProt:RELATED-TO:P19689 , UniProt:RELATED-TO:P23721 , UniProt:RELATED-TO:P33330 , UniProt:RELATED-TO:P44336 , UniProt:RELATED-TO:P62676 , UniProt:RELATED-TO:Q9CHW5 , UniProt:RELATED-TO:Q9PIH3


References

Drewke96: Drewke C, Klein M, Clade D, Arenz A, Muller R, Leistner E (1996). "4-O-phosphoryl-L-threonine, a substrate of the pdxC(serC) gene product involved in vitamin B6 biosynthesis." FEBS Lett 1996;390(2);179-82. PMID: 8706854

Hirsch67: Hirsch H, Greenberg DM (1967). "Studies on phosphoserine aminotransferase of sheep brain." J Biol Chem 242(9);2283-7. PMID: 6022873

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Pizer63: Pizer LI (1963). "The pathway and control of serine biosynthesis in Escherichia coli." J Biol Chem 1963;238:3934-3944. PMID: 14086727

Zhao96: Zhao G, Winkler ME (1996). "A novel alpha-ketoglutarate reductase activity of the serA-encoded 3-phosphoglycerate dehydrogenase of Escherichia coli K-12 and its possible implications for human 2-hydroxyglutaric aciduria." J Bacteriol 1996;178(1);232-9. PMID: 8550422

Zhao96b: Zhao G, Winkler ME (1996). "4-Phospho-hydroxy-L-threonine is an obligatory intermediate in pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli K-12." FEMS Microbiol Lett 1996;135(2-3);275-80. PMID: 8595869


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Thu Nov 27, 2014, BIOCYC14A.