The apo structure of sucrose hydrolase from Xanthomonas campestris pv. campestris shows an open active-site groove

Acta Crystallographica Section D: Biological Crystallography

Volumn 65, Issue 12, 2009, Pages 1309-1314

  Champion, Elise ^a   Remaud Simeon, Magali ^a   Skov, Lars K ^b   Kastrup, Jette S ^c   Gajhede, Michael ^c   Mirza, Osman ^c  

^a UMR792 INGÉNIERIE DES SYSTÈMES BIOLOGIQUES ET DES PROCÉDÉS   (France)

^b NOVOZYMES A S   (Denmark)

^c UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

Active site conformation; Glycoside hydrolase family 13; Reaction mechanism; Sucrose hydrolysis

Indexed keywords

GLYCOSIDASE; SUCROSE;

ARTICLE; BIOCATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYMOLOGY; METABOLISM; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY; XANTHOMONAS CAMPESTRIS;

BIOCATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; GLYCOSIDE HYDROLASES; MODELS, MOLECULAR; PROTEIN STRUCTURE, TERTIARY; SUCROSE; XANTHOMONAS CAMPESTRIS;

XANTHOMONAS AXONOPODIS; XANTHOMONAS CAMPESTRIS; XANTHOMONAS CAMPESTRIS PV. CAMPESTRIS;

EID: 71949109117     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S0907444909040311     Document Type: Article

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