Enzymatic properties and deduced amino acid sequence of a high-alkaline pectate lyase from an alkaliphilic Bacillus isolate

Biochimica et Biophysica Acta - General Subjects

Volumn 1427, Issue 2, 1999, Pages 145-154

  Kobayashi, Tohru ^a   Hatada, Yuji ^a   Higaki, Norihiko ^a   Lusterio, Decorosa D ^a   Ozawa, Tadahiro ^a   Koike, Kenzo ^a   Kawai, Shuji ^a   Ito, Susumu ^a  

^a KAO CORPORATION   (Japan)

Author keywords

Alkaliphile; Bacillus; Cloning; Pectate lyase; Secondary structure prediction; Trans elimination

Indexed keywords

PECTATE LYASE;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS; CLONE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME PURIFICATION; ISOELECTRIC FOCUSING; MOLECULAR CLONING; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE;

AMINO ACID SEQUENCE; BACILLUS; BACTERIAL PROTEINS; CLONING, MOLECULAR; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; POLYSACCHARIDE-LYASES; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY; TEMPERATURE;

EID: 0032908426     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-4165(99)00017-3     Document Type: Article

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