The crystal structure of phosphonate-inhibited D-Ala-D-Ala peptidase reveals an analogue of a tetrahedral transition state

Biochemistry

Volumn 42, Issue 5, 2003, Pages 1199-1208

  Silvaggi, Nicholas R ^a   Anderson, John W ^b   Brinsmade, Shaun R ^a   Pratt, R F ^b   Kelly, Judith A ^a  

^a UNIVERSITY OF CONNECTICUT   (United States)

^b WESLEYAN UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; CATALYSIS; CELLS; CONFORMATIONS; CROSSLINKING; CRYSTAL STRUCTURE; HYDROGEN BONDS; MOLECULES; SUBSTRATES;

MOLECULAR MODELING;

ENZYME INHIBITION;

BETA LACTAM ANTIBIOTIC; DEXTRO ALANINE; DEXTRO ALANYL DEXTRO ALANINE CARBOXYPEPTIDASE; HYDROXYL GROUP; OXYGEN; PEPTIDASE; PEPTIDOGLYCAN; PHOSPHONIC ACID DERIVATIVE; SERINE; TYROSINE; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL CELL WALL; BIOSYNTHESIS; CATALYSIS; CHEMICAL REACTION; CROSS LINKING; CRYSTAL STRUCTURE; DEACYLATION; ENZYME STRUCTURE; HYDROGEN BOND; PRIORITY JOURNAL; STREPTOMYCES;

BETA-LACTAMASES; BINDING SITES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; DIPEPTIDYL PEPTIDASES; OLIGOPEPTIDES; PEPTIDOGLYCAN; PHOSPHONIC ACIDS; PROTEIN CONFORMATION; SERINE PROTEINASE INHIBITORS; STREPTOMYCES; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); STREPTOMYCES;

EID: 0037432016     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0268955     Document Type: Article

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