Analysis of a new crystal form of procarboxypeptidase B: Further insights into the catalytic mechanism

Biopolymers

Volumn 93, Issue 2, 2010, Pages 178-185

  Fernández, Daniel ^a   Boix, Ester ^a   Pallarès, Irantzu ^a   Avilés, Francesc X ^a   Vendrell, Josep ^a  

^a UNIVERSITAT AUTÒNOMA DE BARCELONA   (Spain)

Author keywords

Carboxypeptidase B; Crystal polymorphism; Enzyme mechanism; M14 peptidase family; Sequence analysis; X ray crystallography

Indexed keywords

B-CRYSTALS; BENZAMIDINE; CARBOXYPEPTIDASE; CATALYTIC MECHANISMS; CRYSTAL FORMS; CRYSTAL POLYMORPH; CRYSTALLOGRAPHIC DATA; ENZYME MECHANISM; GENE SEQUENCES; HIGHER RESOLUTION; MOLECULAR PACKINGS; NORMAL MODE ANALYSIS; POLYPEPTIDE CHAIN; PROTEIN STRUCTURES; SEQUENCE ANALYSIS; SUBDOMAIN; SUBSTRATE BINDING; TETRAGONAL CRYSTAL STRUCTURE; TRICLINIC CRYSTAL STRUCTURE; WATER MOLECULE; ZINC IONS;

ENZYMES; MINERALOGY; POLYMORPHISM; RIGID STRUCTURES; SELF ASSEMBLY; X RAY CRYSTALLOGRAPHY; ZINC;

CRYSTAL STRUCTURE;

ALANINE; ARGININE; ASPARAGINE; ASPARTIC ACID; BENZAMIDINE; GLUTAMIC ACID; GLYCINE; HISTIDINE; HYDROGEN; ISOLEUCINE; LEUCINE; LYSINE; METHIONINE; PANCREAS ENZYME; PEPTIDASE; PHENYLALANINE; POLYPEPTIDE; PROCARBOXYPEPTIDASE B; PROLINE; SERINE; THREONINE; TYROSINE; UNCLASSIFIED DRUG; VALINE; WATER; ZINC ION; SOLVENT;

ACCURACY; ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; DNA FLANKING REGION; ENZYME KINETICS; ENZYME SUBSTRATE COMPLEX; GENE SEQUENCE; HYDROGEN BOND; HYDROPHILICITY; HYDROPHOBICITY; NONHUMAN; PREDICTION; PROTEIN DOMAIN; PROTEIN FUNCTION; RESIDUE ANALYSIS; SEQUENCE ANALYSIS; SOLVENT EXTRACTION; SWINE; X RAY CRYSTALLOGRAPHY; BINDING KINETICS; CONTROLLED STUDY; CRYSTALLOGRAPHY; ENZYME ANALYSIS; ENZYME MECHANISM; ENZYME STRUCTURE; NUCLEOTIDE SEQUENCE; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; WATER CONTENT;

SUS;

AMINO ACID SEQUENCE; ANIMALS; CARBOXYPEPTIDASE B; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; HYDROGEN BONDING; HYDROPHOBICITY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; SWINE; ZINC;

EID: 73649102728     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.21320     Document Type: Article

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