The origin of the electrostatic perturbation in acetoacetate decarboxylase

Nature

Volumn 459, Issue 7245, 2009, Pages 393-397

  Ho, Meng Chiao ^a   Ménétret, Jean François ^a   Tsuruta, Hiro ^b   Allen, Karen N ^a,c  

^a BOSTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b SLAC NATIONAL ACCELERATOR LABORATORY   (United States)

^c Boston University   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACETOACETATE DECARBOXYLASE; ACETYLACETONE; CARBOXYLYASE; ENAMINE; LYSINE; NUCLEOPHILE; PROTEIN; UNCLASSIFIED DRUG;

CRYSTAL STRUCTURE; DECARBOXYLATION; ENZYME ACTIVITY; IONIZATION; PERTURBATION; SUBSTRATE; X-RAY;

ARTICLE; CHEMICAL STRUCTURE; DECARBOXYLATION; ELECTROCHEMISTRY; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; HYDROPHOBICITY; PKA; PRIORITY JOURNAL; STEREOSPECIFICITY; X RAY CRYSTALLOGRAPHY;

BIOCATALYSIS; BIPHENYL COMPOUNDS; CARBOXY-LYASES; CATALYTIC DOMAIN; CHROMOBACTERIUM; CLOSTRIDIUM ACETOBUTYLICUM; CRYSTALLOGRAPHY, X-RAY; DECARBOXYLATION; HYDROPHOBICITY; IMIDAZOLES; LYSINE; MODELS, MOLECULAR; PENTANONES; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; STATIC ELECTRICITY;

EID: 66249136708     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature07938     Document Type: Article

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