Pyridoxal kinase

In enzymology, a pyridoxal kinase (EC 2.7.1.35) is an enzyme that catalyzes the chemical reaction

ATP + pyridoxal ${\displaystyle \rightleftharpoons }$ ADP + pyridoxal 5'-phosphate

pyridoxal kinase
Identifiers
EC no.	2.7.1.35
CAS no.	9026-42-0
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

Thus, the two substrates of this enzyme are ATP and pyridoxal, whereas its two products are ADP and pyridoxal 5'-phosphate. A number of other phosphate acceptors can be used in place of pyridoxal to produce the corresponding 5' phosphate, including pyridoxine, pyridoxamine and various derivatives. The 5'-phosphates of pyridoxine and pyridoxamine can be converted to pyridoxal 5'-phosphate by pyridoxine 5′-phosphate oxidase.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:pyridoxal 5'-phosphotransferase. Other names in common use include pyridoxal kinase (phosphorylating), pyridoxal 5-phosphate-kinase, pyridoxal phosphokinase, and pyridoxine kinase. This enzyme participates in vitamin B₆ metabolism.

Humans have one version of this enzyme encoded by the gene PDXK.

Structural studies

As of late 2007, 15 structures have been solved for this class of enzymes, with PDB accession codes 1LHP, 1LHR, 1RFT, 1RFU, 1RFV, 1TD2, 1VI9, 1YGJ, 1YGK, 1YHJ, 2AJP, 2DDM, 2DDO, 2DDW, and 2F7K.