PMID:7592609
| Citation |
Frick, DN, Townsend, BD and Bessman, MJ (1995) A novel GDP-mannose mannosyl hydrolase shares homology with the MutT family of enzymes. J. Biol. Chem. 270:24086-91 |
|---|---|
| Abstract |
The product of the Escherichia coli orf1.9, or yefc, gene (GenBank accession number L11721) has been expressed under the control of a T7 promoter, purified to apparent homogeneity, and identified as a novel enzyme that hydrolyzes GDP-mannose or GDP-glucose to GDP and the respective hexose. The enzyme has little or no activity on other nucleotides, dinucleotides, nucleotide sugars, or sugar phosphates. It has a pH optimum between 9.0 and 9.5, a Km of 0.3 mM, and a Vmax of 1.6 mumol min-1 mg-1 for GDP-mannose, and it requires divalent cations for activity. This enzyme of 160 amino acids (M(r) = 18, 405) contains the consensus sequence GX(I/L/V)(E/Q)(X)2ET(X)6R(X)4E(X)2(I/L), characteristic of the MutT family of proteins and previously shown to form part of the nucleotide-binding site of MutT (Frick, D. N., Weber, D. J., Abeygunawardana, C., Gittis, A. G., Bessman, M. J., and Mildvan, A. S. (1995) Biochemistry 34, 5577-5586). A comparison of the enzymatic reactions catalyzed by the GDP-mannose mannosyl hydrolase and the other enzymes of the MutT family suggests that the consensus signature sequence designates a novel nucleoside diphosphate binding site and catalytic motif. |
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| Keywords |
Amino Acid Sequence; Bacteria/chemistry; Bacteria/genetics; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Base Sequence; Chromosomes, Bacterial; Cloning, Molecular; DNA Primers; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins; Glycoside Hydrolases/chemistry; Glycoside Hydrolases/genetics; Glycoside Hydrolases/metabolism; Humans; Kinetics; Molecular Sequence Data; Phosphoric Monoester Hydrolases/chemistry; Phosphoric Monoester Hydrolases/genetics; Phosphoric Monoester Hydrolases/metabolism; Pyrophosphatases; Recombinant Proteins/chemistry; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism; Sequence Homology, Amino Acid; Substrate Specificity |
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