A new family of carbohydrate esterases is represented by a GDSL hydrolase/acetylxylan esterase from Geobacillus stearothermophilus

Journal of Biological Chemistry

Volumn 286, Issue 49, 2011, Pages 41993-42001

  Alalouf, Onit ^a   Balazs, Yael ^a   Volkinshtein, Margarita ^a   Grimpel, Yael ^a   Shoham, Gil ^b   Shoham, Yuval ^a  

^a TECHNION ISRAEL INSTITUTE OF TECHNOLOGY   (Israel)

^b HEBREW UNIVERSITY OF JERUSALEM   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL GROUPS; CARBOHYDRATE ESTERASE; CATALYTIC TRIAD; DIACETYL; ESTER LINKAGES; GENE PRODUCTS; GEOBACILLUS STEAROTHERMOPHILUS; HYDROLASE FAMILY; IONIZABLE GROUPS; PERACETATE; PHENYL ACETATE; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; SYNTHETIC SUBSTRATES; THERMOPHILIC BACTERIA; TOTAL CORRELATION SPECTROSCOPY; XYLANASES; XYLOBIOSES;

AMINO ACIDS; BACTERIA; ESTERS; GENES; HYDROLYSIS; NAPHTHALENE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SUBSTRATES; SUGARS; VOLATILE FATTY ACIDS;

ENZYMES;

2 NAPHTHYL ACETATE; 4 NITROPHENYL ACETATE; ACETIC ACID 4 METHYLUMBELLIFERYL ESTER; ACETIC ACID DERIVATIVE; ACETIC ACID PHENYL ESTER; ACETYLXYLAN ESTERASE; ASPARTIC ACID; ESTERASE; GDSL HYDROLASE; HISTIDINE; METHYL 2,3,4 TRI O ACETYL BETA XYLOPYRANOSIDE; METHYL 2,3,4,6 TETRA O ACETYL BETA GLUCOPYRANOSIDE; SERINE; SERINE ACETYLXYLAN ESTERASE; UNCLASSIFIED DRUG; XYLOBIOSE PERACETATE; XYLOSE;

ARTICLE; AXE2 GENE; BACTERIAL GENE; CATALYSIS; CONTROLLED STUDY; DEACETYLATION; ENZYME INACTIVATION; ENZYME PURIFICATION; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; GENETIC DATABASE; GEOBACILLUS STEAROTHERMOPHILUS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEOTIDE SEQUENCE; PH; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS;

ACETYLESTERASE; BIOMASS; CARBOHYDRATES; CATALYSIS; CELL WALL; ESTERASES; GEOBACILLUS STEAROTHERMOPHILUS; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; PLANTS; POLYSACCHARIDES; RENEWABLE ENERGY; SERINE PROTEASES; SUBSTRATE SPECIFICITY; XYLANS;

EID: 82755183564     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.301051     Document Type: Article

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