Evolutionary conservation of the substrate-binding cleft of phosphoglycerate kinases.
The primary structures of six phosphoglycerate kinases (PGKs) are known: three from mammals, one from yeast, and two from trypanosomes. Comparison of the amino acid sequence of these enzymes reveals 154 invariant positions out of 392 positions in the aligned sequences. Most of the conserved positions fall into the twelve beta-sheets and adjacent peptide regions that form the inner loops surrounding the ATP and 3-phosphoglycerate-binding cleft. The homology between mammalian and yeast PGKs is greater than 94% for the inner-loop region, even though the overall homology is less than 65%. Trypanosome PGK has only 44% overall homology with the mammalian enzyme, but shows 74% homology in the inner-loop region. Trypanosome PGK contains a polypeptide segment in its N-terminal domain that is transposed in comparison with the other species.
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D005075:Biological Evolution; D002863:Chromogenic Compounds; D006736:Horses; D006801:Humans; D051379:Mice; D010735:Phosphoglycerate Kinase / Q000378:metabolism / Q000502:physiology; D012441:Saccharomyces cerevisiae; D012689:Sequence Homology, Nucleic Acid; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D014346:Trypanosoma brucei brucei
D002863:Chromogenic Compounds; D010735:Phosphoglycerate Kinase