Reaction participants Show >> << Hide
- Name help_outline 2-oxoglutarate Identifier CHEBI:16810 (Beilstein: 3664503; CAS: 64-15-3) help_outline Charge -2 Formula C5H4O5 InChIKeyhelp_outline KPGXRSRHYNQIFN-UHFFFAOYSA-L SMILEShelp_outline [O-]C(=O)CCC(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 425 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline O-phospho-L-serine Identifier CHEBI:57524 Charge -2 Formula C3H6NO6P InChIKeyhelp_outline BZQFBWGGLXLEPQ-REOHCLBHSA-L SMILEShelp_outline [NH3+][C@@H](COP([O-])([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 13 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 3-phosphooxypyruvate Identifier CHEBI:18110 Charge -3 Formula C3H2O7P InChIKeyhelp_outline LFLUCDOSQPJJBE-UHFFFAOYSA-K SMILEShelp_outline [O-]C(=O)C(=O)COP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-glutamate Identifier CHEBI:29985 (CAS: 11070-68-1) help_outline Charge -1 Formula C5H8NO4 InChIKeyhelp_outline WHUUTDBJXJRKMK-VKHMYHEASA-M SMILEShelp_outline [NH3+][C@@H](CCC([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 244 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:14329 | RHEA:14330 | RHEA:14331 | RHEA:14332 | |
---|---|---|---|---|
Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
UniProtKB help_outline |
|
|||
EC numbers help_outline | ||||
Gene Ontology help_outline | ||||
KEGG help_outline | ||||
MetaCyc help_outline | ||||
EcoCyc help_outline | ||||
Reactome help_outline |
Publications
-
THE PATHWAY AND CONTROL OF SERINE BIOSYNTHESIS IN ESCHERICHIA COLI.
PIZER L.I.
J Biol Chem 238:3934-3944(1963) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
-
A critical look at geriatrics in a teaching hospital: Part I. The situation.
Tibbit L.R.
A survey of the admission and discharge patterns of geriatric patients admitted to Groote Schuur Hospital, Cape Town, during July and August 1978 was conducted. The findings highlight a lack of methodology in the economic use of beds, a lack of rehabilitation services and of follow-up services on ... >> More
A survey of the admission and discharge patterns of geriatric patients admitted to Groote Schuur Hospital, Cape Town, during July and August 1978 was conducted. The findings highlight a lack of methodology in the economic use of beds, a lack of rehabilitation services and of follow-up services on discharge, and poor liaison regarding facilities outside the hospital setting. << Less
-
4-O-phosphoryl-L-threonine, a substrate of the pdxC(serC) gene product involved in vitamin B6 biosynthesis.
Drewke C., Klein M., Clade D., Arenz A., Mueller R., Leistner E.
The Escherichia coli pdxC(serC) gene codes for a transaminase (EC 2.6.1.52). The gene is involved in both pyridoxine (vitamin B6) and serine biosynthesis and was overexpressed as a MalE/PdxC(SerC) fusion protein. The fusion protein was purified by affinity chromatography on an amylose resin and hy ... >> More
The Escherichia coli pdxC(serC) gene codes for a transaminase (EC 2.6.1.52). The gene is involved in both pyridoxine (vitamin B6) and serine biosynthesis and was overexpressed as a MalE/PdxC(SerC) fusion protein. The fusion protein was purified by affinity chromatography on an amylose resin and hydrolyzed in the presence of protease factor Xa. Both the fusion protein and the PdxC(SerC) protein were characterized (K(M) value, turnover number, optimum pH). Both enzymes used 4-O-phosphoryl-L-threonine rather than 4-hydroxy-L-threonine as a substrate indicating that the phosphorylated rather than the non-phosphorylated amino acid is involved in pyridoxine biosynthesis. Pyridoxal phosphate was shown to be the cofactor for both enzymes and therefore seems to be involved in its own biosynthesis. << Less
FEBS Lett. 390:179-182(1996) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
-
Studies on phosphoserine aminotransferase of sheep brain.
Hirsch H., Greenberg D.M.
J Biol Chem 242:2283-2287(1967) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
-
4-phospho-hydroxy-L-threonine is an obligatory intermediate in pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli K-12.
Zhao G., Winkler M.E.
We show that thrB-encoded homoserine kinase is required for growth of Escherichia coli K-12 pdxB mutants on minimal glucose medium supplemented with 4-hydroxy-L-threonine (synonym, 3-hydroxyhomoserine) or D-glycolaldehyde. This result is consistent with a model in which 4-phospho-hydroxy-L-threoni ... >> More
We show that thrB-encoded homoserine kinase is required for growth of Escherichia coli K-12 pdxB mutants on minimal glucose medium supplemented with 4-hydroxy-L-threonine (synonym, 3-hydroxyhomoserine) or D-glycolaldehyde. This result is consistent with a model in which 4-phospho-hydroxy-L-threonine (synonym, 3-hydroxyhomoserine phosphate), rather than 4-hydroxy-L-threonine, is an obligatory intermediate in pyridoxal 5'-phosphate biosynthesis. Ring closure using 4-phospho-hydroxy-L-threonine as a substrate would lead to formation of pyridoxine 5'-phosphate, and not pyridoxine, as the first B6-vitamer synthesized de novo. These considerations suggest that E. coli pyridoxal/pyridoxamine/pyridoxine kinase is not required for the main de novo pathway of pyridoxal 5'-phosphate biosynthesis, and instead plays a role only in the B6-vitamer salvage pathway. << Less
FEMS Microbiol. Lett. 135:275-280(1996) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.