| EC Tree |
| 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; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| 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 |
| 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 |
| Title | Authors | Date | PubMed 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 ME | 1998 Apr | 9537380 |
| Expression, purification, and kinetic constants for human and Escherichia coli pyridoxal kinases. | di Salvo ML, Hunt S, Schirch V | 2004 Aug | 15249053 |
| Pyridoxal phosphokinases. I. Assay, distribution, I. Assay, distribution, purification, and properties. | MCCORMICK DB, GREGORY ME, SNELL EE | 1961 Jul | 13773826 |
| 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 |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Expression, purification, and kinetic constants for human and Escherichia coli pyridoxal kinases. | di Salvo ML, Hunt S, Schirch V | 2004 Aug | 15249053 |
| Pyridoxal phosphokinases. I. Assay, distribution, I. Assay, distribution, purification, and properties. | MCCORMICK DB, GREGORY ME, SNELL EE | 1961 Jul | 13773826 |
| 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 |
| Title | Authors | Date | PubMed 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 F | 1998 Dec | 9924807 |
| 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 TP | 2004 Mar | 14973012 |
| 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 ME | 1998 Apr | 9537380 |
| Expression, purification, and kinetic constants for human and Escherichia coli pyridoxal kinases. | di Salvo ML, Hunt S, Schirch V | 2004 Aug | 15249053 |
| Pyridoxal phosphokinases. I. Assay, distribution, I. Assay, distribution, purification, and properties. | MCCORMICK DB, GREGORY ME, SNELL EE | 1961 Jul | 13773826 |