title: Domain organisation in phosphomannose isomerases (types I and II).
abstract: Phosphomannose isomerase (PMI) types I and II were found to possess a conserved protein motif. This motif coincides with the catalytic site of the Candida albicans type I PMI, indicating a common catalytic process for both PMI types. The type II PMI are bifunctional enzymes possessing PMI and guanosine diphospho-D-mannose pyrophosphorylase (GMP) activity in separate catalytic domains, which in some species may function as separate proteins.
authors.affiliation: Department of Microbiology (G08), University of Sydney, NSW, Australia.
authors.forename: S O
authors.initials: SO
authors.lastname: Jensen
authors.forename: P R
authors.initials: PR
authors.lastname: Reeves
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002176:Candida albicans / Q000201:enzymology*; D002384:Catalysis; D017124:Conserved Sequence; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry* / Q000378:metabolism; D008359:Mannose-6-Phosphate Isomerase / Q000737:chemistry* / Q000378:metabolism*; D008969:Molecular Sequence Data; D009713:Nucleotidyltransferases / Q000737:chemistry* / Q000378:metabolism*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
chemical_list: D007527:Isoenzymes; D009713:Nucleotidyltransferases; C026917:mannose 1-phosphate guanylyltransferase; D008359:Mannose-6-Phosphate Isomerase