DB code: S00205

RLCP classification 1.30.36020.973 : Hydrolysis
CATH domain 3.20.20.80 : TIM Barrel Catalytic domain
E.C. 3.2.1.21
CSA 1cbg
M-CSA 1cbg
MACiE

CATH domain Related DB codes (homologues)
3.20.20.80 : TIM Barrel S00202 S00210 S00748 S00906 S00907 S00911 S00912 S00915 M00134 M00160 D00479 S00204 S00206 S00207 S00203 S00208 S00209 S00211 S00213 S00214 M00113 T00307 D00165 D00166 D00169 D00176 D00501 D00502 D00503 D00844 D00861 D00864 M00026 M00112 M00193 M00346 T00057 T00062 T00063 T00066 T00067

Uniprot Enzyme Name
UniprotKB Protein name Synonyms CAZy Pfam RefSeq
P22073 Beta-glucosidase A
BGA
EC 3.2.1.21
Gentiobiase
Cellobiase
Beta-D-glucoside glucohydrolase
Amygdalase
GH1 (Glycoside Hydrolase Family 1)
PF00232 (Glyco_hydro_1)
[Graphical View]
Q03506 Beta-glucosidase
EC 3.2.1.21
Gentiobiase
Cellobiase
Beta-D-glucoside glucohydrolase
Amygdalase
GH1 (Glycoside Hydrolase Family 1)
PF00232 (Glyco_hydro_1)
[Graphical View]
P26205 Cyanogenic beta-glucosidase
EC 3.2.1.21
Linamarase
GH1 (Glycoside Hydrolase Family 1)
PF00232 (Glyco_hydro_1)
[Graphical View]
P49235 Beta-glucosidase, chloroplastic
EC 3.2.1.21
Gentiobiase
Cellobiase
Beta-D-glucoside glucohydrolase
GH1 (Glycoside Hydrolase Family 1)
PF00232 (Glyco_hydro_1)
[Graphical View]
NP_001105454.1 (Protein)
NM_001111984.1 (DNA/RNA sequence)

KEGG enzyme name
beta-glucosidase
gentiobiase
cellobiase
emulsin
elaterase
aryl-beta-glucosidase
beta-D-glucosidase
beta-glucoside glucohydrolase
arbutinase
amygdalinase
p-nitrophenyl beta-glucosidase
primeverosidase
amygdalase
limarase
salicilinase
beta-1,6-glucosidase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P22073 BGLA_PAEPO Hydrolysis of terminal, non-reducing beta-D- glucose residues with release of beta-D-glucose. Homooctamer.
Q03506 BGLA_BACCI Hydrolysis of terminal, non-reducing beta-D- glucosyl residues with release of beta-D-glucose.
P26205 BGLT_TRIRP Hydrolysis of terminal, non-reducing beta-D- glucose residues with release of beta-D-glucose. Homodimer.
P49235 BGLC_MAIZE Hydrolysis of terminal, non-reducing beta-D- glucose residues with release of beta-D-glucose. Homodimer. Plastid, chloroplast.

KEGG Pathways
Map code Pathways E.C.
MAP00460 Cyanoamino acid metabolism
MAP00500 Starch and sucrose metabolism
MAP00940 Phenylpropanoid biosynthesis

Compound table
Substrates Products Intermediates
KEGG-id C00963 C00001 C00963 C00221
E.C.
Compound beta-D-Glucoside H2O beta-D-Glucoside beta-D-Glucose Transition-state in deglycosylation
Type carbohydrate H2O carbohydrate carbohydrate
ChEBI 15377
15903
PubChem 22247451
962
64689
1bgaA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1bgaB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1bgaC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1bgaD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1bggA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1bggB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:GCO
1bggC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:GCO
1bggD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:GCO
1tr1A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1tr1B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1tr1C Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1tr1D Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1qoxA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1qoxB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1qoxC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1qoxD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1qoxE Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1qoxF Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1qoxG Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1qoxH Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1qoxI Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1qoxJ Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1qoxK Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1qoxL Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1qoxM Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1qoxN Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1qoxO Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1qoxP Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1cbgA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1e1eA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1e1eB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1e1fA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:PSG Unbound Unbound
1e1fB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:PSG Unbound Unbound
1e4lA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1e4lB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1e4nA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1e4nB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1e55A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:GLC-DHR Unbound
1e55B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:GLC-DHR Unbound
1e56A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:GLC-HBO Unbound
1e56B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Tansition-state-analogue:GLC-HBO

Reference for Active-site residues
resource references E.C.

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1bgaA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 352
1bgaB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 352
1bgaC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 352
1bgaD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 352
1bggA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 352
1bggB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 352
1bggC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 352
1bggD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 352
1tr1A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 352
1tr1B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 352
1tr1C Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 352
1tr1D Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 352
1qoxA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 355
1qoxB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 355
1qoxC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 355
1qoxD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 355
1qoxE Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 355
1qoxF Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 355
1qoxG Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 355
1qoxH Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 355
1qoxI Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 355
1qoxJ Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 355
1qoxK Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 355
1qoxL Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 355
1qoxM Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 355
1qoxN Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 355
1qoxO Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 355
1qoxP Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 121;GLU 166;TYR 296;GLU 355
1cbgA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 137;GLU 183;TYR 326;GLU 397
1e1eA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 142;GLU 191;TYR 333;GLU 406
1e1eB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 142;GLU 191;TYR 333;GLU 406
1e1fA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 142;GLU 191;TYR 333;GLU 406
1e1fB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 142;GLU 191;TYR 333;GLU 406
1e4lA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 142;;TYR 333;GLU 406 mutant E191D
1e4lB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 142;;TYR 333;GLU 406 mutant E191D
1e4nA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 142;;TYR 333;GLU 406 mutant E191D
1e4nB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 142;;TYR 333;GLU 406 mutant E191D
1e55A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 142;;TYR 333;GLU 406 mutant E191D
1e55B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 142;;TYR 333;GLU 406 mutant E191D
1e56A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 142;;TYR 333;GLU 406 mutant E191D
1e56B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 142;;TYR 333;GLU 406 mutant E191D

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[9]
[10]
[14]
Scheme 1
[15]
p.17175-17176
[16]
Fig.8
[20]
p.495-500
[33]
[34]

References
[1]
Resource
Comments
Medline ID
PubMed ID 1367638
Journal Enzyme Microb Technol
Year 1991
Volume 13
Pages 547-53
Authors Cantarella M, Cantarella L, Alfani F
Title Hydrolytic reactions in two-phase systems. Effect of water-immiscible organic solvents on stability and activity of acid phosphatase, beta-glucosidase, and beta-fructofuranosidase.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 1714449
Journal J Biol Chem
Year 1991
Volume 266
Pages 15021-7
Authors Fabbro D, Grabowski GA
Title 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.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 8477701
Journal Eur J Biochem
Year 1993
Volume 213
Pages 305-12
Authors Kengen SW, Luesink EJ, Stams AJ, Zehnder AJ
Title Purification and characterization of an extremely thermostable beta-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 7986074
Journal Arch Biochem Biophys
Year 1994
Volume 315
Pages 323-30
Authors Keresztessy Z, Kiss L, 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.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 7944386
Journal Arch Biochem Biophys
Year 1994
Volume 314
Pages 142-52
Authors Keresztessy Z, Kiss L, 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.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 8028010
Journal J Mol Biol
Year 1994
Volume 240
Pages 267-70
Authors Sanz-Aparicio J, Romero A, Martinez-Ripoll M, Madarro A, Flors A, Polaina J
Title Crystallization and preliminary X-ray diffraction analysis of a type I beta-glucosidase encoded by the bgIA gene of Bacillus polymyxa.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 8588743
Journal Arch Microbiol
Year 1995
Volume 164
Pages 414-9
Authors Rath J, Messner R, Kosma P, Altmann F, Marz L, Kubicek CP
Title The alpha-D-mannan core of a complex cell-wall heteroglycan of Trichoderma reesei is responsible for beta-glucosidase activation.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 8519777
Journal Biochemistry
Year 1995
Volume 34
Pages 16194-202
Authors Namchuk MN, Withers SG
Title Mechanism of Agrobacterium beta-glucosidase: kinetic analysis of the role of noncovalent enzyme/substrate interactions.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 7578061
Journal Biochemistry
Year 1995
Volume 34
Pages 14554-62
Authors Wang Q, Trimbur D, Graham R, Warren RA, Withers SG
Title Identification of the acid/base catalyst in Agrobacterium faecalis beta-glucosidase by kinetic analysis of mutants.
Related PDB
Related UniProtKB
[10]
Resource
Comments X-ray crystallography (2.15 angstroms).
Medline ID 96097401
PubMed ID 8535788
Journal Structure
Year 1995
Volume 3
Pages 951-60
Authors Barrett T, Suresh CG, Tolley SP, Dodson EJ, Hughes MA
Title The crystal structure of a cyanogenic beta-glucosidase from white clover, a family 1 glycosyl hydrolase.
Related PDB 1cbg
Related UniProtKB P26205
[11]
Resource
Comments
Medline ID
PubMed ID 9636318
Journal Biotechnology (N Y)
Year 1996
Volume 14
Pages 88-91
Authors Fischer L, Bromann R, Kengen SW, de Vos WM, Wagner F
Title Catalytical potency of beta-glucosidase from the extremophile Pyrococcus furiosus in glucoconjugate synthesis.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 9214768
Journal Biosci Biotechnol Biochem
Year 1997
Volume 61
Pages 1033-5
Authors Nunoura N, Fujita T, Ohdan K, Kirihata M, Yamamoto K, Kumagai H
Title Structural analysis of disaccharides synthesized by beta-D-glucosidase of Bifidobacterium breve clb and their assimilation by Bifidobacteria.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 9657966
Journal Biochem J
Year 1998
Volume 333
Pages 275-83
Authors Duroux L, Delmotte FM, Lancelin JM, Keravis G, Jay-Allemand C
Title Insight into naphthoquinone metabolism: beta-glucosidase-catalysed hydrolysis of hydrojuglone beta-D-glucopyranoside.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 9461511
Journal Biochem J
Year 1998
Volume 330
Pages 203-9
Authors Lawson SL, Warren RA, Withers SG
Title Mechanistic consequences of replacing the active-site nucleophile Glu-358 in Agrobacterium sp. beta-glucosidase with a cysteine residue.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 9860830
Journal Biochemistry
Year 1998
Volume 37
Pages 17170-8
Authors Bauer MW, Kelly RM
Title The family 1 beta-glucosidases from Pyrococcus furiosus and Agrobacterium faecalis share a common catalytic mechanism.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 9630531
Journal Biochim Biophys Acta
Year 1998
Volume 1385
Pages 78-88
Authors Watt DK, Ono H, Hayashi K
Title Agrobacterium tumefaciens beta-glucosidase is also an effective beta-xylosidase, and has a high transglycosylation activity in the presence of alcohols.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 9845479
Journal Biol Trace Elem Res
Year 1998
Volume 64
Pages 247-58
Authors Sreekala M, Lalitha K
Title Selenium-mediated differential response of beta-glucosidase and beta-galactosidase of germinating Trigonella foenum-graecum.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 9468315
Journal FEBS Lett
Year 1998
Volume 421
Pages 243-8
Authors Montero E, Vallmitjana M, Perez-Pons JA, Querol E, Jimenez-Barbero J, Canada FJ
Title NMR studies of the conformation of thiocellobiose bound to a beta-glucosidase from Streptomyces sp.
Related PDB
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 9857024
Journal J Biol Chem
Year 1998
Volume 273
Pages 34941-8
Authors Hays WS, VanderJagt DJ, Bose B, Serianni AS, Glew RH
Title Catalytic mechanism and specificity for hydrolysis and transglycosylation reactions of cytosolic beta-glucosidase from guinea pig liver.
Related PDB
Related UniProtKB
[20]
Resource
Comments X-ray crystallography (2.4 angstroms).
Medline ID 98139963
PubMed ID 9466926
Journal J Mol Biol
Year 1998
Volume 275
Pages 491-502
Authors Sanz-Aparicio J, Hermoso JA, Martinez-Ripoll M, Lequerica JL, Polaina J
Title Crystal structure of beta-glucosidase A from Bacillus polymyxa: insights into the catalytic activity in family 1 glycosyl hydrolases.
Related PDB 1bga 1bgg 1tr1
Related UniProtKB P22073
[21]
Resource
Comments
Medline ID
PubMed ID 9849940
Journal Proteins
Year 1998
Volume 33
Pages 567-76
Authors Sanz-Aparicio J, Hermoso JA, Martinez-Ripoll M, Gonzalez B, Lopez-Camacho C, Polaina J
Title Structural basis of increased resistance to thermal denaturation induced by single amino acid substitution in the sequence of beta-glucosidase A from Bacillus polymyxa.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 10467123
Journal Biotechnol Appl Biochem
Year 1999
Volume 30
Pages 81-7
Authors Lin J, Pillay B, Singh S
Title Purification and biochemical characteristics of beta-D-glucosidase from a thermophilic fungus, Thermomyces lanuginosus-SSBP.
Related PDB
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 10583402
Journal Eur J Biochem
Year 1999
Volume 266
Pages 1056-65
Authors Rotrekl V, Nejedla E, Kucera I, Abdallah F, Palme K, Brzobohaty B
Title The role of cysteine residues in structure and enzyme activity of a maize beta-glucosidase.
Related PDB
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 10737327
Journal Glycoconj J
Year 1999
Volume 16
Pages 415-23
Authors Kono H, Kawano S, Tajima K, Erata T, Takai M
Title Structural analyses of new tri- and tetrasaccharides produced from disaccharides by transglycosylation of purified Trichoderma viride beta-glucosidase.
Related PDB
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 10736164
Journal Biochemistry
Year 2000
Volume 39
Pages 3656-65
Authors Lebbink JH, Kaper T, Bron P, van der Oost J, de Vos WM
Title Improving low-temperature catalysis in the hyperthermostable Pyrococcus furiosus beta-glucosidase CelB by directed evolution.
Related PDB
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 11828410
Journal Chembiochem
Year 2000
Volume 1
Pages 177-80
Authors Hansen SU, Plesner IW, Bols M
Title Direct NMR-spectroscopic determination of active-enzyme concentration by titration with a labeled inhibitor: determination of the k(cat) value of almond beta-glucosidase.
Related PDB
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 11052758
Journal J Agric Food Chem
Year 2000
Volume 48
Pages 4929-36
Authors Decker CH, Visser J, Schreier P
Title beta-glucosidases from five black Aspergillus species: study of their physico-chemical and biocatalytic properties.
Related PDB
Related UniProtKB
[28]
Resource
Comments
Medline ID
PubMed ID 10871610
Journal J Biol Chem
Year 2000
Volume 275
Pages 28843-8
Authors Arrizubieta MJ, Polaina J
Title Increased thermal resistance and modification of the catalytic properties of a beta-glucosidase by random mutagenesis and in vitro recombination.
Related PDB
Related UniProtKB
[29]
Resource
Comments X-ray crystallography (2.7 Angstroms)
Medline ID
PubMed ID 10675298
Journal J Struct Biol
Year 2000
Volume 129
Pages 69-79
Authors Hakulinen N, Paavilainen S, Korpela T, Rouvinen J
Title The Crystal Structure of Beta-Glucosidase from Bacillus Circulans Sp. Alkalophilus: Ability to Form Long Polymeric Assemblies.
Related PDB 1qox
Related UniProtKB
[30]
Resource
Comments X-ray crystallography (2.0-2.2 Angstroms)
Medline ID
PubMed ID 11106394
Journal Proc Nat Acad Sci USA
Year 2000
Volume 97
Pages 13555-13560
Authors Czjzek M, Cicek M, Zamboni V, Bevan DR, Henrissat B, Esen A
Title The Mechanism of Substrate (Aglycone) Specificity in Beta-Glucosidases is Revealed by Crystal Structures of Mutant Maize Beta-Glucosidase-Dimboa,-Dimboaglc, and-Dhurrin Complexes.
Related PDB 1e4l 1e4n 1e55 1e56
Related UniProtKB
[31]
Resource
Comments X-ray crystallography (2.5 Angstroms)
Medline ID
PubMed ID 11171077
Journal Biochem J
Year 2001
Volume 354
Pages 37-46
Authors Czjzek M, Cicek M, Zamboni V, Burmeister WP, Bevan DR, Henrissat B, Esen A
Title Crystal Structure of a Monocotyledon (Maize Zmglu1) Beta-Glucosidase and a Model of its Complex with P-Nitrophenyl Beta-D-Thioglucoside.
Related PDB 1e1e 1e1f
Related UniProtKB
[32]
Resource
Comments
Medline ID
PubMed ID 11115405
Journal Biochem J
Year 2001
Volume 353
Pages 117-127
Authors Parry NJ, Beever DE, Owen E, Vandenberghe I, Van Beeumen J, Bhat MK
Title Biochemical characterization and mechanism of action of a thermostable beta-glucosidase purified from Thermoascus aurantiacus.
Related PDB
Related UniProtKB
[33]
Resource
Comments catalysis, kinetics
Medline ID
PubMed ID 11352732
Journal Biochemistry
Year 2001
Volume 40
Pages 5975-82
Authors Vallmitjana M, Ferrer-Navarro M, Planell R, Abel M, Ausin C, Querol E, Planas A, Perez-Pons JA
Title Mechanism of the family 1 beta-glucosidase from Streptomyces sp: catalytic residues and kinetic studies.
Related PDB
Related UniProtKB
[34]
Resource
Comments
Medline ID
PubMed ID 11342030
Journal Biochim Biophys Acta
Year 2001
Volume 1545
Pages 41-52
Authors Marana SR, Jacobs-Lorena M, Terra WR, Ferreira C
Title Amino acid residues involved in substrate binding and catalysis in an insect digestive beta-glycosidase.
Related PDB
Related UniProtKB
[35]
Resource
Comments
Medline ID
PubMed ID 11520685
Journal Insect Biochem Mol Biol
Year 2001
Volume 31
Pages 1065-76
Authors Ferreira AH, Marana SR, Terra WR, Ferreira C
Title Purification, molecular cloning, and properties of a beta-glycosidase isolated from midgut lumen of Tenebrio molitor (Coleoptera) larvae.
Related PDB
Related UniProtKB
[36]
Resource
Comments
Medline ID
PubMed ID 11706179
Journal Plant Physiol
Year 2001
Volume 127
Pages 973-85
Authors Zouhar J, Vevodova J, Marek J, Damborsky J, Su XD, Brzobohaty B
Title Insights into the functional architecture of the catalytic center of a maize beta-glucosidase Zm-p60.1.
Related PDB
Related UniProtKB
[37]
Resource
Comments
Medline ID
PubMed ID 12450115
Journal Biosci Biotechnol Biochem
Year 2002
Volume 66
Pages 2060-7
Authors Fukuda K, Mori H, Okuyama M, Kimura A, Ozaki H, Yoneyama M, Chiba S
Title Identification of essential ionizable groups and evaluation of subsite affinities in the active site of beta-D-glucosidase F1 from a Streptomyces sp.
Related PDB
Related UniProtKB
[38]
Resource
Comments
Medline ID
PubMed ID 12363364
Journal Biotechnol Prog
Year 2002
Volume 18
Pages 1104-8
Authors Maugard T, Enaud E, de la Sayette A, Choisy P, Legoy MD
Title Beta-glucosidase-catalyzed hydrolysis of indican from leaves of Polygonum tinctorium.
Related PDB
Related UniProtKB

Comments
This enzyme belongs to the family-1 of glycosidase enzymes, a member family of 4/7 superfamily, which has got the catalytic residues at the C-terminal ends of beta-4 and beta-7 on the (alpha/beta)8 barrel fold.
According to the literature [10] & [20], Glu352 and Glu166 (of PDB;1bgaA) act as a nucleophile and an acid-base, respectively. Moreover, the literature suggested that His121 might stabilize the transition-state, and that Tyr296 modulates the pKa and the activity of the nucleophile, Glu352.

Created Updated
2003-12-05 2009-03-17