S00205
type: Enzyme
rlcp: p973
cath: TIM Barrel
ec: https://purl.uniprot.org/enzyme/3.2.1.21
csa: 1cbg
uniprot: P22073
uniprot: Q03506
uniprot: P26205
uniprot: P49235
kegg enzyme: beta-glucosidase
kegg pathway: Cyanoamino acid metabolism
kegg pathway: Starch and sucrose metabolism
kegg pathway: Phenylpropanoid biosynthesis
kegg substrate: beta-D-Glucoside
kegg substrate: H2O
kegg product: beta-D-Glucoside
kegg product: beta-D-Glucose
pdb: 1bgaA
pdb: 1bgaB
pdb: 1bgaC
pdb: 1bgaD
pdb: 1bggA
pdb: 1bggB
pdb: 1bggC
pdb: 1bggD
pdb: 1tr1A
pdb: 1tr1B
pdb: 1tr1C
pdb: 1tr1D
pdb: 1qoxA
pdb: 1qoxB
pdb: 1qoxC
pdb: 1qoxD
pdb: 1qoxE
pdb: 1qoxF
pdb: 1qoxG
pdb: 1qoxH
pdb: 1qoxI
pdb: 1qoxJ
pdb: 1qoxK
pdb: 1qoxL
pdb: 1qoxM
pdb: 1qoxN
pdb: 1qoxO
pdb: 1qoxP
pdb: 1cbgA
pdb: 1e1eA
pdb: 1e1eB
pdb: 1e1fA
pdb: 1e1fB
pdb: 1e4lA
pdb: 1e4lB
pdb: 1e4nA
pdb: 1e4nB
pdb: 1e55A
pdb: 1e55B
pdb: 1e56A
pdb: 1e56B
references: Hydrolytic reactions in two-phase systems. Effect of water-immiscible organic solvents on stability and activity of acid phosphatase, beta-glucosidase, and beta-fructofuranosidase.
references: Human acid beta-glucosidase. Use of inhibitory and activating monoclonal antibodies to investigate the enzyme's catalytic mechanism and saposin A and C binding sites.
references: Purification and characterization of an extremely thermostable beta-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus.
references: http://ezcatdb.cbrc.jp/EzCatDB/reference/S00205#4
references: http://ezcatdb.cbrc.jp/EzCatDB/reference/S00205#5
references: Crystallization and preliminary X-ray diffraction analysis of a type I beta-glucosidase encoded by the bgIA gene of Bacillus polymyxa.
references: The alpha-D-mannan core of a complex cell-wall heteroglycan of Trichoderma reesei is responsible for beta-glucosidase activation.
references: Mechanism of Agrobacterium beta-glucosidase: kinetic analysis of the role of noncovalent enzyme/substrate interactions.
references: Identification of the acid/base catalyst in Agrobacterium faecalis beta-glucosidase by kinetic analysis of mutants.
references: The crystal structure of a cyanogenic beta-glucosidase from white clover, a family 1 glycosyl hydrolase.
references: Catalytical potency of beta-glucosidase from the extremophile Pyrococcus furiosus in glucoconjugate synthesis.
references: Structural analysis of disaccharides synthesized by beta-D-glucosidase of Bifidobacterium breve clb and their assimilation by Bifidobacteria.
references: Insight into naphthoquinone metabolism: beta-glucosidase-catalysed hydrolysis of hydrojuglone beta-D-glucopyranoside.
references: Mechanistic consequences of replacing the active-site nucleophile Glu-358 in Agrobacterium sp. beta-glucosidase with a cysteine residue.
references: The family 1 beta-glucosidases from Pyrococcus furiosus and Agrobacterium faecalis share a common catalytic mechanism.
references: Agrobacterium tumefaciens beta-glucosidase is also an effective beta-xylosidase, and has a high transglycosylation activity in the presence of alcohols.
references: Selenium-mediated differential response of beta-glucosidase and beta-galactosidase of germinating Trigonella foenum-graecum.
references: NMR studies of the conformation of thiocellobiose bound to a beta-glucosidase from Streptomyces sp.
references: Catalytic mechanism and specificity for hydrolysis and transglycosylation reactions of cytosolic beta-glucosidase from guinea pig liver.
references: Crystal structure of beta-glucosidase A from Bacillus polymyxa: insights into the catalytic activity in family 1 glycosyl hydrolases.
references: Structural basis of increased resistance to thermal denaturation induced by single amino acid substitution in the sequence of beta-glucosidase A from Bacillus polymyxa.
references: Purification and biochemical characteristics of beta-D-glucosidase from a thermophilic fungus, Thermomyces lanuginosus-SSBP.

TIM Barrel
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.20.20.80
catalytic domain: index.html

Cyanoamino acid metabolism
type: KeggPathway
references: KEGG:MAP00460

Starch and sucrose metabolism
type: KeggPathway
references: KEGG:MAP00500

Phenylpropanoid biosynthesis
type: KeggPathway
references: KEGG:MAP00940

beta-D-Glucoside
type: KeggSubstrate
type: KeggProduct
references: KEGG:C00963
compound type: carbohydrate

H2O
type: KeggSubstrate
references: KEGG:C00001
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: H2O

beta-D-Glucose
type: KeggProduct
references: KEGG:C00221
references: CHEBI:15903
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: carbohydrate

1bgaA
type: Pdb
references: 1bga
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bga
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 352

1bgaB
type: Pdb
references: 1bga
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bga
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 352

1bgaC
type: Pdb
references: 1bga
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bga
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 352

1bgaD
type: Pdb
references: 1bga
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bga
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 352

1bggA
type: Pdb
references: 1bgg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bgg
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 352

1bggB
type: Pdb
references: 1bgg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bgg
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 352

1bggC
type: Pdb
references: 1bgg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bgg
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 352

1bggD
type: Pdb
references: 1bgg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bgg
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 352

1tr1A
type: Pdb
references: 1tr1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tr1
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 352

1tr1B
type: Pdb
references: 1tr1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tr1
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 352

1tr1C
type: Pdb
references: 1tr1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tr1
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 352

1tr1D
type: Pdb
references: 1tr1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tr1
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 352

1qoxA
type: Pdb
references: 1qox
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qox
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 355

1qoxB
type: Pdb
references: 1qox
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qox
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 355

1qoxC
type: Pdb
references: 1qox
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qox
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 355

1qoxD
type: Pdb
references: 1qox
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qox
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 355

1qoxE
type: Pdb
references: 1qox
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qox
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 355

1qoxF
type: Pdb
references: 1qox
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qox
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 355

1qoxG
type: Pdb
references: 1qox
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qox
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 355

1qoxH
type: Pdb
references: 1qox
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qox
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 355

1qoxI
type: Pdb
references: 1qox
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qox
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 355

1qoxJ
type: Pdb
references: 1qox
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qox
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 355

1qoxK
type: Pdb
references: 1qox
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qox
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 355

1qoxL
type: Pdb
references: 1qox
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qox
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 355

1qoxM
type: Pdb
references: 1qox
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qox
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 355

1qoxN
type: Pdb
references: 1qox
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qox
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 355

1qoxO
type: Pdb
references: 1qox
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qox
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 355

1qoxP
type: Pdb
references: 1qox
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qox
catalytic residue: HIS 121;GLU 166;TYR 296;GLU 355

1cbgA
type: Pdb
references: 1cbg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cbg
catalytic residue: HIS 137;GLU 183;TYR 326;GLU 397

1e1eA
type: Pdb
references: 1e1e
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e1e
catalytic residue: HIS 142;GLU 191;TYR 333;GLU 406

1e1eB
type: Pdb
references: 1e1e
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e1e
catalytic residue: HIS 142;GLU 191;TYR 333;GLU 406

1e1fA
type: Pdb
references: 1e1f
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e1f
catalytic residue: HIS 142;GLU 191;TYR 333;GLU 406

1e1fB
type: Pdb
references: 1e1f
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e1f
catalytic residue: HIS 142;GLU 191;TYR 333;GLU 406

1e4lA
type: Pdb
references: 1e4l
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e4l
catalytic residue: HIS 142; ;TYR 333;GLU 406
comment: mutant E191D

1e4lB
type: Pdb
references: 1e4l
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e4l
catalytic residue: HIS 142; ;TYR 333;GLU 406
comment: mutant E191D

1e4nA
type: Pdb
references: 1e4n
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e4n
catalytic residue: HIS 142; ;TYR 333;GLU 406
comment: mutant E191D

1e4nB
type: Pdb
references: 1e4n
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e4n
catalytic residue: HIS 142; ;TYR 333;GLU 406
comment: mutant E191D

1e55A
type: Pdb
references: 1e55
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e55
catalytic residue: HIS 142; ;TYR 333;GLU 406
comment: mutant E191D

1e55B
type: Pdb
references: 1e55
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e55
catalytic residue: HIS 142; ;TYR 333;GLU 406
comment: mutant E191D

1e56A
type: Pdb
references: 1e56
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e56
catalytic residue: HIS 142; ;TYR 333;GLU 406
comment: mutant E191D

1e56B
type: Pdb
references: 1e56
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e56
catalytic residue: HIS 142; ;TYR 333;GLU 406
comment: mutant E191D

Hydrolytic reactions in two-phase systems. Effect of water-immiscible organic solvents on stability and activity of acid phosphatase, beta-glucosidase, and beta-fructofuranosidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1367638
journal: Enzyme Microb Technol
volume: 13
pages: 547-53
published year: 1991
authors:
  item: Cantarella M
  item: Cantarella L
  item: Alfani F

Human acid beta-glucosidase. Use of inhibitory and activating monoclonal antibodies to investigate the enzyme's catalytic mechanism and saposin A and C binding sites.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1714449
journal: J Biol Chem
volume: 266
pages: 15021-7
published year: 1991
authors:
  item: Fabbro D
  item: Grabowski GA

Purification and characterization of an extremely thermostable beta-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8477701
journal: Eur J Biochem
volume: 213
pages: 305-12
published year: 1993
authors:
  item: Kengen SW
  item: Luesink EJ
  item: Stams AJ
  item: Zehnder AJ

http://ezcatdb.cbrc.jp/EzCatDB/reference/S00205#4
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7986074
journal: Arch Biochem Biophys
volume: 315
pages: 323-30
published year: 1994
authors:
  item: Keresztessy Z
  item: Kiss L
  item: Hughes MA
title: Investigation of the active site of the cyanogenic beta-D-glucosidase (linamarase) from Manihot esculenta Crantz (cassava). II. Identification of Glu-198 as an active site carboxylate group with acid catalytic function.

http://ezcatdb.cbrc.jp/EzCatDB/reference/S00205#5
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7944386
journal: Arch Biochem Biophys
volume: 314
pages: 142-52
published year: 1994
authors:
  item: Keresztessy Z
  item: Kiss L
  item: Hughes MA
title: Investigation of the active site of the cyanogenic beta-D-glucosidase (linamarase) from Manihot esculenta Crantz (cassava). I. Evidence for an essential carboxylate and a reactive histidine residue in a single catalytic center.

Crystallization and preliminary X-ray diffraction analysis of a type I beta-glucosidase encoded by the bgIA gene of Bacillus polymyxa.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8028010
journal: J Mol Biol
volume: 240
pages: 267-70
published year: 1994
authors:
  item: Sanz-Aparicio J
  item: Romero A
  item: Martinez-Ripoll M
  item: Madarro A
  item: Flors A
  item: Polaina J

The alpha-D-mannan core of a complex cell-wall heteroglycan of Trichoderma reesei is responsible for beta-glucosidase activation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8588743
journal: Arch Microbiol
volume: 164
pages: 414-9
published year: 1995
authors:
  item: Rath J
  item: Messner R
  item: Kosma P
  item: Altmann F
  item: Marz L
  item: Kubicek CP

Mechanism of Agrobacterium beta-glucosidase: kinetic analysis of the role of noncovalent enzyme/substrate interactions.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8519777
journal: Biochemistry
volume: 34
pages: 16194-202
published year: 1995
authors:
  item: Namchuk MN
  item: Withers SG

Identification of the acid/base catalyst in Agrobacterium faecalis beta-glucosidase by kinetic analysis of mutants.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7578061
journal: Biochemistry
volume: 34
pages: 14554-62
published year: 1995
authors:
  item: Wang Q
  item: Trimbur D
  item: Graham R
  item: Warren RA
  item: Withers SG

The crystal structure of a cyanogenic beta-glucosidase from white clover, a family 1 glycosyl hydrolase.
type: BibliographicResource
comment: X-ray crystallography (2.15 angstroms).
medline id: 96097401
references: http://www.ncbi.nlm.nih.gov/pubmed/8535788
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P26205
journal: Structure
volume: 3
pages: 951-60
published year: 1995
authors:
  item: Barrett T
  item: Suresh CG
  item: Tolley SP
  item: Dodson EJ
  item: Hughes MA

Catalytical potency of beta-glucosidase from the extremophile Pyrococcus furiosus in glucoconjugate synthesis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9636318
journal: Biotechnology (N Y)
volume: 14
pages: 88-91
published year: 1996
authors:
  item: Fischer L
  item: Bromann R
  item: Kengen SW
  item: de Vos WM
  item: Wagner F

Structural analysis of disaccharides synthesized by beta-D-glucosidase of Bifidobacterium breve clb and their assimilation by Bifidobacteria.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9214768
journal: Biosci Biotechnol Biochem
volume: 61
pages: 1033-5
published year: 1997
authors:
  item: Nunoura N
  item: Fujita T
  item: Ohdan K
  item: Kirihata M
  item: Yamamoto K
  item: Kumagai H

Insight into naphthoquinone metabolism: beta-glucosidase-catalysed hydrolysis of hydrojuglone beta-D-glucopyranoside.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9657966
journal: Biochem J
volume: 333
pages: 275-83
published year: 1998
authors:
  item: Duroux L
  item: Delmotte FM
  item: Lancelin JM
  item: Keravis G
  item: Jay-Allemand C

Mechanistic consequences of replacing the active-site nucleophile Glu-358 in Agrobacterium sp. beta-glucosidase with a cysteine residue.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9461511
journal: Biochem J
volume: 330
pages: 203-9
published year: 1998
authors:
  item: Lawson SL
  item: Warren RA
  item: Withers SG

The family 1 beta-glucosidases from Pyrococcus furiosus and Agrobacterium faecalis share a common catalytic mechanism.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9860830
journal: Biochemistry
volume: 37
pages: 17170-8
published year: 1998
authors:
  item: Bauer MW
  item: Kelly RM

Agrobacterium tumefaciens beta-glucosidase is also an effective beta-xylosidase, and has a high transglycosylation activity in the presence of alcohols.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9630531
journal: Biochim Biophys Acta
volume: 1385
pages: 78-88
published year: 1998
authors:
  item: Watt DK
  item: Ono H
  item: Hayashi K

Selenium-mediated differential response of beta-glucosidase and beta-galactosidase of germinating Trigonella foenum-graecum.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9845479
journal: Biol Trace Elem Res
volume: 64
pages: 247-58
published year: 1998
authors:
  item: Sreekala M
  item: Lalitha K

NMR studies of the conformation of thiocellobiose bound to a beta-glucosidase from Streptomyces sp.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9468315
journal: FEBS Lett
volume: 421
pages: 243-8
published year: 1998
authors:
  item: Montero E
  item: Vallmitjana M
  item: Perez-Pons JA
  item: Querol E
  item: Jimenez-Barbero J
  item: Canada FJ

Catalytic mechanism and specificity for hydrolysis and transglycosylation reactions of cytosolic beta-glucosidase from guinea pig liver.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9857024
journal: J Biol Chem
volume: 273
pages: 34941-8
published year: 1998
authors:
  item: Hays WS
  item: VanderJagt DJ
  item: Bose B
  item: Serianni AS
  item: Glew RH

Crystal structure of beta-glucosidase A from Bacillus polymyxa: insights into the catalytic activity in family 1 glycosyl hydrolases.
type: BibliographicResource
comment: X-ray crystallography (2.4 angstroms).
medline id: 98139963
references: http://www.ncbi.nlm.nih.gov/pubmed/9466926
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P22073
journal: J Mol Biol
volume: 275
pages: 491-502
published year: 1998
authors:
  item: Sanz-Aparicio J
  item: Hermoso JA
  item: Martinez-Ripoll M
  item: Lequerica JL
  item: Polaina J

Structural basis of increased resistance to thermal denaturation induced by single amino acid substitution in the sequence of beta-glucosidase A from Bacillus polymyxa.
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Purification and biochemical characteristics of beta-D-glucosidase from a thermophilic fungus, Thermomyces lanuginosus-SSBP.
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The role of cysteine residues in structure and enzyme activity of a maize beta-glucosidase.
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pages: 1056-65
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Structural analyses of new tri- and tetrasaccharides produced from disaccharides by transglycosylation of purified Trichoderma viride beta-glucosidase.
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Improving low-temperature catalysis in the hyperthermostable Pyrococcus furiosus beta-glucosidase CelB by directed evolution.
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volume: 39
pages: 3656-65
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authors:
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Direct NMR-spectroscopic determination of active-enzyme concentration by titration with a labeled inhibitor: determination of the k(cat) value of almond beta-glucosidase.
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volume: 1
pages: 177-80
published year: 2000
authors:
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beta-glucosidases from five black Aspergillus species: study of their physico-chemical and biocatalytic properties.
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volume: 48
pages: 4929-36
published year: 2000
authors:
  item: Decker CH
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Increased thermal resistance and modification of the catalytic properties of a beta-glucosidase by random mutagenesis and in vitro recombination.
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journal: J Biol Chem
volume: 275
pages: 28843-8
published year: 2000
authors:
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The Crystal Structure of Beta-Glucosidase from Bacillus Circulans Sp. Alkalophilus: Ability to Form Long Polymeric Assemblies.
type: BibliographicResource
comment: X-ray crystallography (2.7 Angstroms)
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journal: J Struct Biol
volume: 129
pages: 69-79
published year: 2000
authors:
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The Mechanism of Substrate (Aglycone) Specificity in Beta-Glucosidases is Revealed by Crystal Structures of Mutant Maize Beta-Glucosidase-Dimboa,-Dimboaglc, and-Dhurrin Complexes.
type: BibliographicResource
comment: X-ray crystallography (2.0-2.2 Angstroms)
references: http://www.ncbi.nlm.nih.gov/pubmed/11106394
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pages: 13555-13560
published year: 2000
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Crystal Structure of a Monocotyledon (Maize Zmglu1) Beta-Glucosidase and a Model of its Complex with P-Nitrophenyl Beta-D-Thioglucoside.
type: BibliographicResource
comment: X-ray crystallography (2.5 Angstroms)
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Biochemical characterization and mechanism of action of a thermostable beta-glucosidase purified from Thermoascus aurantiacus.
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Mechanism of the family 1 beta-glucosidase from Streptomyces sp: catalytic residues and kinetic studies.
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Amino acid residues involved in substrate binding and catalysis in an insect digestive beta-glycosidase.
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Purification, molecular cloning, and properties of a beta-glycosidase isolated from midgut lumen of Tenebrio molitor (Coleoptera) larvae.
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pages: 1065-76
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Insights into the functional architecture of the catalytic center of a maize beta-glucosidase Zm-p60.1.
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Identification of essential ionizable groups and evaluation of subsite affinities in the active site of beta-D-glucosidase F1 from a Streptomyces sp.
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Beta-glucosidase-catalyzed hydrolysis of indican from leaves of Polygonum tinctorium.
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gentiobiase
type: KeggEnzyme

cellobiase
type: KeggEnzyme

emulsin
type: KeggEnzyme

elaterase
type: KeggEnzyme

aryl-beta-glucosidase
type: KeggEnzyme

beta-D-glucosidase
type: KeggEnzyme

beta-glucoside glucohydrolase
type: KeggEnzyme

arbutinase
type: KeggEnzyme

amygdalinase
type: KeggEnzyme

p-nitrophenyl beta-glucosidase
type: KeggEnzyme

primeverosidase
type: KeggEnzyme

amygdalase
type: KeggEnzyme

limarase
type: KeggEnzyme

salicilinase
type: KeggEnzyme

beta-1,6-glucosidase
type: KeggEnzyme

Analogue
compound: beta-D-Glucoside
pdb: 1e1fA
ligand het code: PSG

Analogue
compound: beta-D-Glucoside
pdb: 1e1fB
ligand het code: PSG

Analogue
compound: beta-D-Glucoside
pdb: 1e55A
ligand het code: GLC-DHR

Analogue
compound: beta-D-Glucoside
pdb: 1e55B
ligand het code: GLC-DHR

Analogue
compound: beta-D-Glucoside
pdb: 1e56A
ligand het code: GLC-HBO

Analogue
compound: beta-D-Glucose
pdb: 1bggB
ligand het code: GCO

Analogue
compound: beta-D-Glucose
pdb: 1bggC
ligand het code: GCO

Analogue
compound: beta-D-Glucose
pdb: 1bggD
ligand het code: GCO

TransitionStateAnalogue
pdb: 1e56B
ligand het code: GLC-HBO

ReferenceForCatalyticMechanism
reference index: 9

ReferenceForCatalyticMechanism
reference index: 10

ReferenceForCatalyticMechanism
reference index: 14
reference section: Scheme 1

ReferenceForCatalyticMechanism
reference index: 15
reference section: p.17175-17176

ReferenceForCatalyticMechanism
reference index: 16
reference section: Fig.8

ReferenceForCatalyticMechanism
reference index: 20
reference section: p.495-500

ReferenceForCatalyticMechanism
reference index: 33

ReferenceForCatalyticMechanism
reference index: 34