Glucose-6-phosphate dehydrogenase. Characterization of a reactive lysine residue in the Pichia jadinii enzyme reveals a limited structural variation in a functionally significant segment.
Glucose-6-phosphate dehydrogenase from the yeast Pichia jadinii has a reactive lysine residue in a segment of amino acid sequence Ile-Asp-His-Tyr-Leu-Gly-Lys*-Glu-Met-Val-Lys. This structure differs from that of other characterized glucose-6-phosphate dehydrogenases, but outside yeasts the segment is invariant in known mammalian, insect and bacterial forms. Thus, limited structural variation is now defined within yeasts for a part of the protein otherwise strictly conserved, and for which stringent structural requirements probably relate to enzymic mechanisms.
Jeffery
J
J
Department of Biochemistry, University of Aberdeen, Marischal College, Scotland, UK.
Wood
I
I
Macleod
A
A
Jeffery
R
R
Jörnvall
H
H
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001241:Aspirin / Q000494:pharmacology; D002175:Candida / Q000201:enzymology*; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D005954:Glucosephosphate Dehydrogenase / Q000032:analysis* / Q000037:antagonists & inhibitors; D008239:Lysine; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D012689:Sequence Homology, Nucleic Acid; D014357:Trypsin
D000596:Amino Acids; D010446:Peptide Fragments; D005954:Glucosephosphate Dehydrogenase; D014357:Trypsin; D008239:Lysine; D001241:Aspirin