A single Gly114Arg mutation stabilizes the hexameric subunit assembly and changes the substrate specificity of halo-archaeal nucleoside diphosphate kinase

FEBS Letters

Volumn 581, Issue 21, 2007, Pages 4073-4079

  Ishibashi, Matsujiro ^a   Tatsuda, Shuhei ^a   Izutsu, Ken ichi ^b   Kumeda, Kouko ^a   Arakawa, Tsutomu ^c   Tokunaga, Masao ^a  

^a KAGOSHIMA UNIVERSITY   (Japan)

^b NATIONAL INSTITUTE OF HEALTH SCIENCES   (Japan)

^c ALLIANCE PROTEIN LABORATORIES   (United States)

Author keywords

Extremely halophilic archaea; Halophilic; Mutation; Nucleoside diphosphate kinase; Substrate specificity; Subunit assembly

Indexed keywords

GLYCINE; MUTANT PROTEIN; NUCLEOSIDE DIPHOSPHATE KINASE; SODIUM CHLORIDE;

ARCHAEBACTERIUM; ARTICLE; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME STABILITY; ESCHERICHIA COLI; GEL PERMEATION CHROMATOGRAPHY; LIGHT SCATTERING; MOLECULAR WEIGHT; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; TEMPERATURE DEPENDENCE; THERMOSTABILITY; WILD TYPE;

AMINO ACID SUBSTITUTION; ARCHAEAL PROTEINS; CATALYTIC DOMAIN; HALOBACTERIUM SALINARUM; MUTATION, MISSENSE; NUCLEOSIDE-DIPHOSPHATE KINASE; PROTEIN FOLDING; SODIUM CHLORIDE; SUBSTRATE SPECIFICITY;

ARCHAEA; ESCHERICHIA COLI;

EID: 34547692741     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.07.042     Document Type: Article

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