Pyridoxal kinase

• Cat.No.: CBCRY19

Specification

• Source: E.coli
• Tag: Non
• 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.
• Protein Classification: Transferase
• Structure Weight: 74135.20 Da
• Polymer: 1
• Molecule: Pyridoxal kinase
• Chain Length: 327 amino acids
• PDB ID: 2F7K
• MMDB ID: 39840
• Method: X-Ray Diffraction
• Resolution: 2.8Å
• Reference: Cao, P., Gong, Y., Tang, L., Leung, Y.C., Jiang, T.(2006) Crystal structure of human pyridoxal kinaseJ.Struct.Biol.154: 327-332

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
• Gene ID: 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