2.6.1.52: phosphoserine transaminase

This is an abbreviated version!
For detailed information about phosphoserine transaminase, go to the full flat file.

Reaction

Synonyms

3-O-phospho-L-serine:2-oxoglutarate aminotransferase, 3-phosphoserine aminotransferase, AspAT, AtPSAT, AtPSAT1, BCIR PSAT, bmPSAT, EhPSAT, hydroxypyruvic phosphate-glutamic transaminase, L-phosphoserine aminotransferase, phosphohydroxypyruvate transaminase, phosphohydroxypyruvic-glutamic transaminase, phosphoserine aminotransferase, phosphoserine aminotransferase 1, phosphoserine aminotransferase1, phosphoserine aminotransferase2, phosphoserine aminotransferases, PSAT, PSAT alpha, PSAT beta, PSAT-BALC, PSAT-BCIRA, PSAT-ECOLI, PSAT1, PSAT2, PSerAT, serC, sll1559

ECTree

     2 Transferases

         2.6 Transferring nitrogenous groups

             2.6.1 Transaminases

                2.6.1.52 phosphoserine transaminase

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Results	in table
34262	AA Sequence
7	Application
1	CAS Registry Number
23	Cloned(Commentary)
25	Cofactor
10	Crystallization (Commentary)
266	Disease/ Diagnostics
5	Expression
32	General Information
3	General Stability
1	IC50 Value
13	Inhibitors
4	kcat/KM [mM/s]
4	Ki Value [mM]
60	KM Value [mM]
10	Localization
31	Molecular Weight [Da]
28	Natural Substrates/ Products (Substrates)
65	Organism
14	Pathway
77	PDB ID
21	pH Optimum
10	pH Range
1	pH Stability
7	pI Value
35	Protein Variants
21	Purification (Commentary)
4	Reaction
1	Reaction Type
58	Reference
57	Source Tissue
43	Specific Activity [micromol/min/mg]
3	Storage Stability
74	Substrates and Products (Substrate)
21	Subunits
96	Synonyms
1	Systematic Name
6	Temperature Optimum [°C]
3	Temperature Stability [°C]
10	Turnover Number [1/s]

Systematic Name

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Systematic Name on EC 2.6.1.52 - phosphoserine transaminase

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SYSTEMATIC NAME

IUBMB Comments

O-phospho-L-serine:2-oxoglutarate aminotransferase

A pyridoxal 5'-phosphate protein. This enzyme catalyses the second step in the phosphorylated pathway of serine biosynthesis [1,3] and the third step in pyridoxal 5'-phosphate biosynthesis in the bacterium Escherichia coli [3]. Pyridoxal 5'-phosphate is the cofactor for both activities and therefore seems to be involved in its own biosynthesis [4]. Non-phosphorylated forms of serine and threonine are not substrates [4]. The archaeal enzyme has a relaxed specificity and can act on L-cysteate and L-alanine as alternative substrates to O-phospho-L-serine [7].