The conserved N-terminal helix of acylpeptide hydrolase from archaeon Aeropyrum pernix K1 is important for its hyperthermophilic activity

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1784, Issue 9, 2008, Pages 1176-1183

  Zhang, Zuoming ^a   Zheng, Baisong ^a   Wang, Yanping ^a   Chen, Yiqian ^a   Manco, Giuseppe ^b   Feng, Yan ^a  

^a JILIN UNIVERSITY   (China)

^b INSTITUTE OF PROTEIN BIOCHEMISTRY   (Italy)

Author keywords

Acylpeptide hydrolase; Molecular dynamics simulation; N terminal truncation; Prolyl oligopeptidase family; Protein stability

Indexed keywords

ACYLAMINO ACID RELEASING ENZYME; ACYLAMINOACYL PEPTIDASE; ACYLAMINOACYL-PEPTIDASE; ARCHAEAL DNA; PEPTIDE HYDROLASE; PRIMER DNA;

AEROPYRUM; AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIAL SURVIVAL; BIOPHYSICS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME STABILITY; GENE DELETION; HYDROPHOBICITY; HYPERTHERMOPHILIC ARCHAEON; NONHUMAN; PRIORITY JOURNAL; PROTEIN ENGINEERING; THERMODYNAMICS; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; GENETICS; HEAT; METABOLISM; MOLECULAR GENETICS; MUTAGENESIS; NUCLEOTIDE SEQUENCE; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN SECONDARY STRUCTURE; SEQUENCE HOMOLOGY;

AEROPYRUM PERNIX; ARCHAEA;

AEROPYRUM; AMINO ACID SEQUENCE; BASE SEQUENCE; CONSERVED SEQUENCE; DNA PRIMERS; DNA, ARCHAEAL; ENZYME STABILITY; HEAT; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS; PEPTIDE HYDROLASES; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; SEQUENCE DELETION; SEQUENCE HOMOLOGY, AMINO ACID; THERMODYNAMICS;

EID: 53149110079     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.05.011     Document Type: Article

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