Hydrophilic residues surrounding the S1 and S2 pockets contribute to dimerisation and catalysis in human dipeptidyl peptidase 8 (DP8)

Biological Chemistry

Volumn 391, Issue 8, 2010, Pages 959-972

  Pitman, Melissa R ^a   Menz, R Ian ^a   Abbott, Catherine A ^a  

^a FLINDERS UNIVERSITY   (Australia)

Author keywords

Active site; Dipeptidyl peptidase; Fibroblast activation protein; Homology modelling; Substrate specificity

Indexed keywords

ALPHA BETA HYDROLASE; DIMER; DIPEPTIDYL PEPTIDASE; DIPEPTIDYL PEPTIDASE 8; DIPEPTIDYL PEPTIDASE 8 INHIBITOR; FIBROBLAST ACTIVATION PROTEIN; HYDROLASE; PEPTIDE HYDROLASE INHIBITOR; PROTEIN; UNCLASSIFIED DRUG;

BIOCATALYSIS; CONFERENCE PAPER; CRYSTAL STRUCTURE; DIMERIZATION; ENZYME ACTIVITY; ENZYME LOCALIZATION; GEL PERMEATION CHROMATOGRAPHY; GENE MUTATION; HYDROPHILICITY; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN;

BIOCATALYSIS; CATALYTIC DOMAIN; DATABASES, PROTEIN; DIMERIZATION; DIPEPTIDASES; DIPEPTIDYL PEPTIDASE 4; DIPEPTIDYL-PEPTIDASES AND TRIPEPTIDYL-PEPTIDASES; GELATINASES; HUMANS; HYDROGEN-ION CONCENTRATION; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; KINETICS; MEMBRANE PROTEINS; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN STABILITY; PROTEIN STRUCTURE, QUATERNARY; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SERINE ENDOPEPTIDASES; SUBSTRATE SPECIFICITY;

EID: 77955944761     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2010.111     Document Type: Conference Paper

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