Cat. No.

CBCRY19

Background

Pyridoxal kinase, a member of the ribokinase superfamily, catalyzes the ATP-dependent phosphorylation reaction of vitamin B6 and is an essential enzyme in the formation of pyridoxal-5'-phosphate, a key cofactor for over 100 enzymes. Pyridoxal kinase is thus regarded as a potential target for pharmacological agents. Structure comparison reveals that the key 12-residue peptide over the active site in HPLK is a beta-strand/loop/beta-strand flap, while the corresponding peptide in sheep brain enzyme adopts a loop conformation. Moreover, HPLK possesses a more hydrophobic ATP-binding pocket.

Molecular description

Protein Classification

Transferase

Structure Weight

74135.20 Da

Polymer

1

Molecule

Pyridoxal kinase

Chain Length

327 amino acids

Crystal Description

PDB ID

2F7K

MMDB ID

39840

Source

E.coli

Method

X-Ray Diffraction

Resolution

2.8Å

Gene information

Gene Name

PDXK

Synonyms

C21orf124; C21orf97; EC 2.7.1.35; DKFZp566A071; FLJ31940; FLJ37311; FLJ21324; MGC15873; MGC31754; MGC52346; PKH; PNK; PRED79; pyridoxal kinase; pyridoxamine kinase; pyridoxine kinase; vitamin B6 kinase; chromosome 21 open reading reame 124; chromosome 21 open reading frame 97

UniProt ID

O00764

GeneID

8566

Chromosome  Location

21q22.3

Function

ATP binding; lithium ion binding; magnesium ion binding; nucleotide binding; potassium ion binding; protein homodimerization activity; pyridoxal kinase activity; sodium ion binding; transferase activity; zinc ion binding

Reference

Cao, P.,  Gong, Y.,  Tang, L.,  Leung, Y.C.,  Jiang, T. (2006) Crystal structure of human pyridoxal kinase J.Struct.Biol. 154: 327-332