Structure, function, and evolution of phosphoglycerate mutases: Comparison with fructose-2,6-bisphosphatase, acid phosphatase, and alkaline phosphatase

Progress in Biophysics and Molecular Biology

Volumn 73, Issue 2-4, 2000, Pages 263-287

  Jedrzejas, M J ^a  

^a University of Alabama at Birmingham   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACID PHOSPHATASE; ALKALINE PHOSPHATASE; FRUCTOSE 2,6 BISPHOSPHATASE; FRUCTOSE 2,6 BISPHOSPHATE 2 PHOSPHATASE; FRUCTOSE-2,6-BISPHOSPHATE 2-PHOSPHATASE; ISOENZYME; PHOSPHATASE; PHOSPHOGLYCERATE MUTASE;

AMINO ACID SEQUENCE; BACILLUS STEAROTHERMOPHILUS; BINDING SITE; CATALYSIS; CHEMICAL STRUCTURE; COMPARATIVE STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; HUMAN; MOLECULAR EVOLUTION; MOLECULAR GENETICS; MOLECULAR MODEL; NONHUMAN; PROTEIN SECONDARY STRUCTURE; REVIEW; SACCHAROMYCES CEREVISIAE; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; SPECIES DIFFERENCE;

ACID PHOSPHATASE; ALKALINE PHOSPHATASE; AMINO ACID SEQUENCE; BACILLUS STEAROTHERMOPHILUS; BINDING SITES; EVOLUTION, MOLECULAR; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHOSPHOFRUCTOKINASE-2; PHOSPHOGLYCERATE MUTASE; PHOSPHORIC MONOESTER HYDROLASES; PROTEIN STRUCTURE, SECONDARY; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY, AMINO ACID;

GEOBACILLUS STEAROTHERMOPHILUS; SACCHAROMYCES CEREVISIAE;

EID: 0033819024     PISSN: 00796107     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0079-6107(00)00007-9     Document Type: Review

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