Domain organisation in phosphomannose isomerases (types I and II).
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.
Jensen
S O
SO
Department of Microbiology (G08), University of Sydney, NSW, Australia.
Reeves
P R
PR
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
D007527:Isoenzymes; D009713:Nucleotidyltransferases; C026917:mannose 1-phosphate guanylyltransferase; D008359:Mannose-6-Phosphate Isomerase