Crystal structures of Bacillus caldovelox arginase in complex with substrate and inhibitors reveal new insights into activation, inhibition and catalysis in the arginase superfamily

Structure

Volumn 7, Issue 4, 1999, Pages 435-448

  Bewley, Maria C ^a,c   Jeffrey, Philip D ^a,d   Patchett, Mark L ^a   Kanyo, Zoltan F ^b,e   Baker, Edward N ^a,f  

^a MASSEY UNIVERSITY   (New Zealand)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

^c BROOKHAVEN NATIONAL LABORATORY   (United States)

^d MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

^e UNIVERSITY OF CALIFORNIA   (United States)

^f UNIVERSITY OF AUCKLAND   (New Zealand)

Author keywords

Arginine hydrolysis; Catalytic mechanism; Crystal structure; Ligand binding; Manganese enzyme; Nitrogen metabolism

Indexed keywords

ARGINASE;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ASSAY; ENZYME CONFORMATION; ENZYME INHIBITION; ENZYME SUBSTRATE COMPLEX; ENZYME SYNTHESIS; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL;

ANIMALIA; BACILLUS CALDOVELOX;

EID: 0033561427     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(99)80056-2     Document Type: Article

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