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Volumn 10, Issue 9, 2001, Pages 1835-1846
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A cofactor-dependent phosphoglycerate mutase homolog from Bacillus stearothermophilus is actually a broad specificity phosphatase
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Author keywords
Bacillus; Functional genomics; Molecular modeling; Phosphatase; Phosphoglycerate mutase homolog; Structure function relationship; Structure prediction
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Indexed keywords
PHOSPHATASE;
PHOSPHOGLYCERATE MUTASE;
ARTICLE;
BACILLUS SUBTILIS;
CRYSTAL STRUCTURE;
ENZYME ACTIVITY;
ENZYME ANALYSIS;
ENZYME ASSAY;
ENZYME LOCALIZATION;
ENZYME SPECIFICITY;
GENE OVEREXPRESSION;
GENE SEQUENCE;
GENOME;
GEOBACILLUS STEAROTHERMOPHILUS;
MOLECULAR MODEL;
NONHUMAN;
NUCLEOTIDE SEQUENCE;
PHYLOGENY;
PRIORITY JOURNAL;
SEQUENCE ANALYSIS;
STRUCTURE ACTIVITY RELATION;
STRUCTURE ANALYSIS;
AMINO ACID SEQUENCE;
BACILLUS STEAROTHERMOPHILUS;
BACILLUS SUBTILIS;
COENZYMES;
CONSENSUS SEQUENCE;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
MULTIENZYME COMPLEXES;
PHOSPHOGLYCERATE MUTASE;
PHOSPHOPROTEIN PHOSPHATASE;
PHYLOGENY;
PROTEIN CONFORMATION;
SEQUENCE ALIGNMENT;
SEQUENCE HOMOLOGY, AMINO ACID;
STRUCTURE-ACTIVITY RELATIONSHIP;
SUBSTRATE SPECIFICITY;
BACILLUS SUBTILIS;
BACTERIA (MICROORGANISMS);
GEOBACILLUS STEAROTHERMOPHILUS;
POSIBACTERIA;
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EID: 0034848174
PISSN: 09618368
EISSN: None
Source Type: Journal
DOI: 10.1110/ps.15701 Document Type: Article |
Times cited : (45)
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References (60)
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