Enzyme

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     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.1 Phosphotransferases with an alcohol group as acceptor
ID:2.7.1.35
Description:Pyridoxal kinase.
Alternative Name: Vitamin B6 kinase.
Vitamin B(6) kinase.
Pyridoxine kinase.
Pyridoxamine kinase.
Cath: 3.40.1190.20;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.1.35
BRENDA Enzyme Link: BRENDA 2.7.1.35
KEGG Enzyme Link: KEGG2.7.1.35
BioCyc Enzyme Link: BioCyc 2.7.1.35
ExPASy Enzyme Link: ExPASy2.7.1.35
EC2PDB Enzyme Link: EC2PDB 2.7.1.35
ExplorEnz Enzyme Link: ExplorEnz 2.7.1.35
PRIAM enzyme-specific profiles Link: PRIAM 2.7.1.35
IntEnz Enzyme Link: IntEnz 2.7.1.35
MEDLINE Enzyme Link: MEDLINE 2.7.1.35
MSA:

2.7.1.35;

Phylogenetic Tree:

2.7.1.35;

Uniprot:
M-CSA:
RHEA:25108 ATP + pyridoxine = ADP + H(+) + pyridoxine 5'-phosphate
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:8]-[OH;+0:7].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Identification and function of the pdxY gene, which encodes a novel pyridoxal kinase involved in the salvage pathway of pyridoxal 5'-phosphate biosynthesis in Escherichia coli K-12.Yang Y, Tsui HC, Man TK, Winkler ME1998 Apr9537380
Expression, purification, and kinetic constants for human and Escherichia coli pyridoxal kinases.di Salvo ML, Hunt S, Schirch V2004 Aug15249053
Pyridoxal phosphokinases. I. Assay, distribution, I. Assay, distribution, purification, and properties.MCCORMICK DB, GREGORY ME, SNELL EE1961 Jul13773826

RHEA:25104 ATP + pyridoxamine = ADP + H(+) + pyridoxamine 5'-phosphate
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:8]-[OH;+0:7].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Expression, purification, and kinetic constants for human and Escherichia coli pyridoxal kinases.di Salvo ML, Hunt S, Schirch V2004 Aug15249053
Pyridoxal phosphokinases. I. Assay, distribution, I. Assay, distribution, purification, and properties.MCCORMICK DB, GREGORY ME, SNELL EE1961 Jul13773826

RHEA:10224 ATP + pyridoxal = ADP + H(+) + pyridoxal 5'-phosphate
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:8]-[OH;+0:7].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Porcine pyridoxal kinase c-DNA cloning, expression and confirmation of its primary sequence.Gao ZG, Lau CK, Lo SC, Choi SY, Churchich JE, Kwok F1998 Dec9924807
Characterization of two kinases involved in thiamine pyrophosphate and pyridoxal phosphate biosynthesis in Bacillus subtilis: 4-amino-5-hydroxymethyl-2methylpyrimidine kinase and pyridoxal kinase.Park JH, Burns K, Kinsland C, Begley TP2004 Mar14973012
Identification and function of the pdxY gene, which encodes a novel pyridoxal kinase involved in the salvage pathway of pyridoxal 5'-phosphate biosynthesis in Escherichia coli K-12.Yang Y, Tsui HC, Man TK, Winkler ME1998 Apr9537380
Expression, purification, and kinetic constants for human and Escherichia coli pyridoxal kinases.di Salvo ML, Hunt S, Schirch V2004 Aug15249053
Pyridoxal phosphokinases. I. Assay, distribution, I. Assay, distribution, purification, and properties.MCCORMICK DB, GREGORY ME, SNELL EE1961 Jul13773826