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You searched for: Publication Year 2010 Remove constraint Publication Year: 2010 Subject active sites Remove constraint Subject: active sites Subject term beta-glucosidase Remove constraint Subject term: beta-glucosidase Text Availability Citation in PubAg Remove constraint Text Availability: Citation in PubAg
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1. A cold-active β-glucosidase (Bgl1C) from a sea bacteria Exiguobacterium oxidotolerans A011

Author:
Chen, Shuilian; Hong, Yuzhi; Shao, Zongze; Liu, Ziduo
Source:
World journal of microbiology & biotechnology 2010 v.26 no.8 pp. 1427-1435
ISSN:
0959-3993
Subject:
EDTA (chelating agent); Exiguobacterium; active sites; alanine; amino acid sequences; bacteria; beta-glucosidase; buffers; calcium; cobalt; copper; genes; genomic libraries; industrial applications; mercury; molecular weight; nucleotides; open reading frames; pH; serine; sodium; temperature; valine
Abstract:
... By constructing a genomic library, a new gene encoding β-glucosidase (Bgl1C) was cloned from Exiguobacterium oxidotolerans A011, which was isolated from deep sea mud. The putative β-glucosidase gene consisted of an open reading frame (ORF) of 1,347 nucleotides, and encoded a protein of 448 amino acids with a predicted molecular weight of 51.6 kDa. Bgl1C belonged to the glycoside hydrolase family 1 ...
DOI:
10.1007/s11274-010-0317-7

2. A new β-glucosidase gene from the zygomycete fungus Rhizomucor miehei

Author:
Takó, Miklós; Tóth, Adél; Nagy, László G.; Krisch, Judit; Vágvölgyi, Csaba; Papp, Tamás
Source:
Antonie van Leeuwenhoek 2010 v.97 no.1 pp. 1-10
ISSN:
0003-6072
Subject:
Mucor; proteins; Rhizomucor miehei; plasmids; amino acids; active sites; introns; sequence homology; beta-glucosidase; fungi
Abstract:
... In this study, a β-glucosidase coding gene (bgl) of the zygomycete fungus Rhizomucor miehei has been cloned and characterized. The gene comprises a total of 2,826 bp including the coding sequence of a 717 amino acids length putative protein and 10 introns dispersed in the whole coding region. The putative N-and C-terminal catalytic domains (aa 68 to aa 274 and aa 358-601, respectively) were identi ...
DOI:
10.1007/s10482-009-9382-z

3. β-Glucosidases

Author:
Ketudat Cairns, James R.; Esen, Asim
Source:
Cellular and molecular life sciences 2010 v.67 no.20 pp. 3389-3405
ISSN:
1420-682X
Subject:
active sites; amino acid sequences; animals; aromatic compounds; beta-glucans; beta-glucosidase; biomass; cell walls; glycosides; industrial applications; lignification; metabolism; microorganisms; plant hormones; proteins
Abstract:
... β-Glucosidases (3.2.1.21) are found in all domains of living organisms, where they play essential roles in the removal of nonreducing terminal glucosyl residues from saccharides and glycosides. β-Glucosidases function in glycolipid and exogenous glycoside metabolism in animals, defense, cell wall lignification, cell wall β-glucan turnover, phytohormone activation, and release of aromatic compounds ...
DOI:
10.1007/s00018-010-0399-2
PubMed:
20490603