Pro-sequence and Ca2+-binding: Implications for folding and maturation of Ntn-hydrolase penicillin amidase from E. coli

Journal of Molecular Biology

Volumn 348, Issue 4, 2005, Pages 999-1014

  Ignatova, Zoya ^a   Wischnewski, Frank ^a   Notbohm, Holger ^b   Kasche, Volker ^a  

^a HAMBURG UNIVERSITY OF TECHNOLOGY   (Germany)

^b UNIVERSITY OF LÜBECK   (Germany)

Author keywords

Ca2+; Folding intermediate; Penicillin amidase; Pro peptide; Protein folding

Indexed keywords

CALCIUM ION; PENICILLIN AMIDASE; PROTEIN PRECURSOR; AMIDASE; CALCIUM; N TERMINAL NUCLEOPHILE HYDROLASE; N-TERMINAL NUCLEOPHILE HYDROLASE; UREA;

ALCALIGENES FAECALIS; ALPHA HELIX; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CALCIUM BINDING; CIRCULAR DICHROISM; CONTROLLED STUDY; ENZYME MECHANISM; ESCHERICHIA COLI; GEL PERMEATION CHROMATOGRAPHY; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY; STRUCTURE ANALYSIS; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME STABILITY; ENZYMOLOGY; GENETICS; KINETICS; METABOLISM; MOLECULAR GENETICS; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; THERMODYNAMICS;

AMIDOHYDROLASES; AMINO ACID SEQUENCE; BINDING SITES; CALCIUM; ENZYME STABILITY; ESCHERICHIA COLI; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PENICILLIN AMIDASE; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; THERMODYNAMICS; UREA;

EID: 17444429637     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.03.005     Document Type: Article

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