The active site architecture of Pisum sativum β-carbonic anhydrase is a mirror image of that of α-carbonic anhydrases

EMBO Journal

Volumn 19, Issue 7, 2000, Pages 1407-1418

  Kimber, Matthew S ^a,c   Pai, Emil F ^a,b,c  

^a UNIVERSITY OF TORONTO   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

^c Networks of Centres of Excellence   (Canada)

Author keywords

carbonic anhydrase; Convergent evolution; X ray crystallography; Zinc enzyme

Indexed keywords

ACETIC ACID; ALPHA CARBONATE DEHYDRATASE; ARGININE; ASPARTIC ACID; BETA CARBONATE DEHYDRATASE; CARBONATE DEHYDRATASE; CYSTEINE; DIMER; GLUTAMINE; GLYCINE; HISTIDINE; ISOENZYME; PHENYLALANINE; TYROSINE; UNCLASSIFIED DRUG; VALINE; ZINC ION;

ARTICLE; BINDING SITE; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME MECHANISM; ENZYME STRUCTURE; NONHUMAN; PLANT; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN FOLDING;

AMINO ACID SEQUENCE; CARBONIC ANHYDRASES; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ELECTROSTATICS; LIGANDS; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEAS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

PISUM SATIVUM; SATIVUM;

EID: 0034599484     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

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