Porcine pyridoxal kinase c-DNA cloning, expression and confirmation of its primary sequence.

  title={Porcine pyridoxal kinase c-DNA cloning, expression and confirmation of its primary sequence.},
  author={Z. G. Gao and Chi-kong Lau and Samuel Chun-lap Lo and S. Y. Choi and Jorge E. Churchich and Francis Kwok},
  journal={The international journal of biochemistry \& cell biology},
  volume={30 12},
  • Z. GaoC. Lau F. Kwok
  • Published 1 December 1998
  • Biology
  • The international journal of biochemistry & cell biology

Molecular Cloning and Catalytic Properties of Human Brain Pyridoxal Kinase

Results from intrinsic fluorescence quenching measurements showed that the tryptophanyl residues in the recombinant protein are more accessible to the neutral acrylamide than to the negatively charged iodide.

Bombyx mori pyridoxal kinase cDNA cloning and enzymatic characterization.

Cloning and characterization of Arabidopsis thaliana pyridoxal kinase

Results from the present study suggest that plant tissues depend on PK for the production of PLP, and examination of levels of enzyme expression showed that leaves, stems, roots and flowers can generate PLP independently at similar levels.

Pyridoxal kinase knockout of Dictyostelium complemented by the human homologue.

Phylogenetic analysis indicated that the Dictyostelium amino acid sequence was closer to human pyridoxal kinase than to pyridine kinases of lower eukaryotes.

Recombinant expression, purification and characterization of Bombyx mori (Lepidoptera: Bombycidae) pyridoxal kinase

Pyridoxal kinase (PLK; EC 2.7.35) is a key enzyme in the metabolism of vitamin B6 (VB6) in Bombyx mori and a double reciprocal plot of initial velocity suggests that the enzyme catalyses the reaction by means of a sequential catalytic mecha- nism.

Functional significance of some particular amino acid residues in Bombyx mori pyridoxal kinase.

Biochemistry and Molecular Biology of Vitamin B6 and PQQ-dependent Proteins

Genetic, Genomic Approaches for Delineating the Pathway of Pyridoxal 5'-Phosphate Coenzyme Biosynthesis in Escherichia coli, and Biological Implications of the Different Hsp70 Binding Properties of Mitochondrial, Cytosolic Aspartate Aminotransferase.



Human Pyridoxal Kinase

Peptide fragments of a porcine benzodiazepine-binding protein were used to isolate the cDNA of a related human protein. The cDNA encodes a polypeptide of 312 amino acid residues that is homologous to

Identification and Functional Characterization of an Active-site Lysine in Mevalonate Kinase*

  • D. PotterJean M. WojnarChakravarthy NarasimhanHenry M. Miziorko
  • Biology, Chemistry
    The Journal of Biological Chemistry
  • 1997
The construction of an expression plasmid for rat mevalonate kinase and the overexpression of recombinant enzyme in Escherichia coli are reported and the observed 56-fold diminution in affinity for the mutant enzyme supports an additional role for lysine 13 in stabilization of ATP binding.

Brain pyridoxal kinase. Purification and characterization.

Results obtained from electron microscopy, using a negative staining technique, provide evidence that pyridoxal kinase exists as a dispherical subunit structure, and indicates that it is a dimeric enzyme.

Brain pyridoxal kinase. Mobility of the substrate pyridoxal and binding of inhibitors to the nucleotide site.

Results are consistent with the hypothesis that N-dansyl-2-oxopyrrolidine binds at the nucleotide binding site of pyridoxal kinase, and reveal that the substrate is not rigidly trapped by the protein matrix.

Analysis of the sequence of amino acids surrounding sites of tyrosine phosphorylation.

The single phosphorylated tyrosine in p60src, the transforming protein of Rous sarcoma virus, is identified as part of the sequence NH2-Arg-Leu-Ile-Glu-Asp-Asn-GLU-Tyr(P)-Thr-Ala- Arg-COOH, a sequence that is recognized efficiently by a tyrosin protein kinase in vivo.

Identification of the pdxK gene that encodes pyridoxine (vitamin B6) kinase in Escherichia coli K-12.

The amino acid sequence of pdxK has signature motifs of the PfkB superfamily of carbohydrate kinases, which includes phosphofructokinases and ribokinases, and suggests that three unidentified ORFs of Salmonella typhimurium, Haemophilus influenzae, and Saccharomyces cerevisiae correspond to PN/PL/PM kinases.

Cloning and characterization of ERG8, an essential gene of Saccharomyces cerevisiae that encodes phosphomevalonate kinase

expression of the ERG8 gene in S. cerevisiae from the galactose-inducible galactokinase (GAL1) promoter resulted in 1,000-fold-elevated levels of phosphomevalonate kinase enzyme activity, indicating that this gene is essential.

Brain pyridoxal kinase: photoaffinity labeling of the substrate-binding site.