"PDXK" Related Products

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Pyridoxal kinase

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.
Protein Classification: Transferase
Structure Weight: 74135.20 Da
Polymer: 1
Molecule: Pyridoxal kinase
Chain Length: 327 amino acids
PDB ID: 2F7K
MMDB ID: 39840
Source: E.coli
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 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

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Optional requirements on this protein    +Expand
C-fusion    N-fusion   Non-tagged
His    GST   Fc   Others
<1.0 eu/μg    <0.1 eu/μg   <0.01 eu/μg   Not required
Monomer Isolation    Dimer Isolation    Not required
>80% by SDS-PAGE    >90% by SDS-PAGE   >95% by SDS-PAGE   Others

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