The unique glycoside hydrolase family 77 amylomaltase from Borrelia burgdorferi with only catalytic triad conserved

FEMS Microbiology Letters

Volumn 284, Issue 1, 2008, Pages 84-91

  Godány, Andrej ^a   Vidová, Barbora ^a   Janeček, Štefan ^a  

^a INSTITUTE OF CHEMISTRY   (Slovakia)

Author keywords

amylase family; Borrelia burgdorferi; Catalytic triad; Evolutionary relationships

Indexed keywords

4ALPHA GLUCANOTRANSFERASE; ARGININE; BACTERIAL DNA; BACTERIAL PROTEIN; GH77 ENZYME; GLUCOSE; GLYCOSIDASE; HYDROLASE; OLIGOSACCHARIDE; PROTEIN MAIQ; RECOMBINANT PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; BACTERIAL STRAIN; BIOINFORMATICS; BORRELIA BURGDORFERI; CATALYSIS; DNA SEQUENCE; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE AMPLIFICATION; GENETIC CONSERVATION; GLYCOSYLATION; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYACRYLAMIDE GEL ELECTROPHORESIS; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BORRELIA BURGDORFERI; CATALYTIC DOMAIN; CLONING, MOLECULAR; CONSERVED SEQUENCE; DNA, BACTERIAL; ESCHERICHIA COLI; GENE EXPRESSION; GLUCOSE; GLYCOGEN DEBRANCHING ENZYME SYSTEM; MOLECULAR SEQUENCE DATA; OLIGOSACCHARIDES; PHYLOGENY; POLYMERASE CHAIN REACTION; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, DNA; SEQUENCE HOMOLOGY, AMINO ACID;

BORRELIA BURGDORFERI; ESCHERICHIA COLI; PROKARYOTA; SPIROCHAETA;

EID: 44649096836     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1111/j.1574-6968.2008.01191.x     Document Type: Article

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