EzCatDB: S00511

DB codeS00511
RLCP classification1.30.36300.2
CATH domainDomain 12.60.120.200Catalytic domain
E.C.3.2.1.73
CSA2ayh

CATH domainRelated DB codes (homologues)
2.60.120.200S00148,D00535,D00666,M00185,T00064,T00208

Enzyme Name
Swiss-protKEGG

P27051P23904
Protein nameBeta-glucanaseBeta-glucanaselicheninase
lichenase
beta-(1->4)-D-glucan 4-glucanohydrolase
1,3
1,4-beta-glucan endohydrolase
1,3
1,4-beta-glucan 4-glucanohydrolase
1,3-1,4-beta-D-glucan 4-glucanohydrolase
SynonymsEC 3.2.1.73
Endo-beta-1,3-1,4 glucanase
1,3-1,4-beta-D-glucan 4-glucanohydrolase
Lichenase
EC 3.2.1.73
Endo-beta-1,3-1,4 glucanase
1,3-1,4-beta-D-glucan 4-glucanohydrolase
Lichenase


Swiss-prot:Accession NumberP27051P23904
Entry nameGUB_BACLIGUB_PAEMA
ActivityHydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds.Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds.
Subunit

Subcellular location

Cofactor



SubstratesProducts
KEGG-idC00551C00478C00001C00551
Compoundbeta-D-GlucanLicheninH2Obeta-D-Glucan
TypepolysaccharidecarbohydrateH2Opolysaccharide
1gbgAUnboundUnbound
Unbound
1ajkAUnboundUnbound
Unbound
1ajkBUnboundUnbound
Unbound
1ajoAUnboundUnbound
Unbound
1ajoBUnboundUnbound
Unbound
1byhAUnboundUnbound
Analogue:NBU-GLC-BGC
1cpmAUnboundUnbound
Unbound
1cpnAUnboundUnbound
Unbound
1glhAUnboundUnbound
Unbound
1macAUnboundUnbound
Unbound
1macBUnboundUnbound
Unbound
2ayhAUnboundUnbound
Unbound
1axkA01UnboundUnbound
Unbound
1axkB01UnboundUnbound
Unbound

Active-site residues
resource
Swiss-prot;P23904, P45797
pdbCatalytic residues
1gbgAGLU 105;GLU 109
1ajkAGLU  22;GLU  26
1ajkBGLU  22;GLU  26
1ajoAGLU 193;GLU 197
1ajoBGLU 193;GLU 197
1byhAGLU 105;GLU 109
1cpmAGLU  47;GLU  51
1cpnAGLU  47;GLU  51
1glhAGLU 105;GLU 109
1macAGLU 103;GLU 107
1macBGLU 103;GLU 107
2ayhAGLU 105;GLU 109
1axkA01GLU  47;GLU  51
1axkB01GLU  47;GLU  51

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[6]

[8]p.14534
[11]Fig.8, p.853-8542
[15]Scheme 1, p.138464
[16]Scheme 2, p.113404
[18]Scheme 1a2
[22]Fig.5, Fig.10, p.3694
[24]Scheme 1, p.794
[26]p.2394

references
[1]
PubMed ID1904865
JournalJ Biol Chem
Year1991
Volume266
Pages11628-31
AuthorsHoj PB, Rodriguez EB, Iser JR, Stick RV, Stone BA
TitleActive site-directed inhibition by optically pure epoxyalkyl cellobiosides reveals differences in active site geometry of two 1,3-1,4-beta-D-glucan 4-glucanohydrolases. The importance of epoxide stereochemistry for enzyme inactivation.
[2]
PubMed ID2023245
JournalJ Mol Biol
Year1991
Volume218
Pages703-4
AuthorsKeitel T, Granzin J, Simon O, Borriss R, Thomsen KK, Wessner H, Hohne W, Heinemann U
TitleCrystallization of the hybrid Bacillus (1-3,1-4)-beta-glucanase H(A16-M).
[3]
PubMed ID1354172
JournalFEBS Lett
Year1992
Volume308
Pages141-5
AuthorsPlanas A, Juncosa M, Lloberas J, Querol E
TitleEssential catalytic role of Glu134 in endo-beta-1,3-1,4-D-glucan 4-glucanohydrolase from B. licheniformis as determined by site-directed mutagenesis.
[4]
CommentsACTIVE SITE.
Medline ID93094208
PubMed ID1360982
JournalJ Biol Chem
Year1992
Volume267
Pages25059-66
AuthorsHoj PB, Condron R, Traeger JC, McAuliffe JC, Stone BA
TitleIdentification of glutamic acid 105 at the active site of Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan 4-glucanohydrolase using epoxide-based inhibitors.
Related Swiss-protP23904
[5]
PubMed ID8280073
JournalBiochem J
Year1993
Volume296
Pages753-8
AuthorsMalet C, Jimenez-Barbero J, Bernabe M, Brosa C, Planas A
TitleStereochemical course and structure of the products of the enzymic action of endo-1,3-1,4-beta-D-glucan 4-glucanohydrolase from Bacillus licheniformis.
[6]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Medline ID93281743
PubMed ID8099449
JournalProc Natl Acad Sci U S A
Year1993
Volume90
Pages5287-91
AuthorsKeitel T, Simon O, Borriss R, Heinemann U
TitleMolecular and active-site structure of a Bacillus 1,3-1,4-beta-glucanase.
Related PDB1byh
Related Swiss-protP23904
[7]
CommentsX-ray crystallography
PubMed ID8200344
JournalEur J Biochem
Year1994
Volume222
Pages203-14
AuthorsKeitel T, Meldgaard M, Heinemann U
TitleCation binding to a Bacillus (1,3-1,4)-beta-glucanase. Geometry, affinity and effect on protein stability.
Related PDB1glh
[8]
PubMed ID8182059
JournalJ Biol Chem
Year1994
Volume269
Pages14530-5
AuthorsJuncosa M, Pons J, Dot T, Querol E, Planas A
TitleIdentification of active site carboxylic residues in Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase by site-directed mutagenesis.
[9]
PubMed ID8162185
JournalMicrobiology
Year1994
Volume140
Pages159-66
AuthorsMeldgaard M, Svendsen I
TitleDifferent effects of N-glycosylation on the thermostability of highly homologous bacterial (1,3-1,4)-beta-glucanases secreted from yeast.
[10]
CommentsX-ray crystallography
PubMed ID7937966
JournalProc Natl Acad Sci U S A
Year1994
Volume91
Pages10417-21
AuthorsHahn M, Piotukh K, Borriss R, Heinemann U
TitleNative-like in vivo folding of a circularly permuted jellyroll protein shown by crystal structure analysis.
Related PDB1cpm,1cpn
[11]
CommentsX-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
Medline ID96028129
PubMed ID7588726
JournalEur J Biochem
Year1995
Volume232
Pages849-58
AuthorsHahn M, Keitel T, Heinemann U
TitleCrystal and molecular structure at 0.16-nm resolution of the hybrid Bacillus endo-1,3-1,4-beta-D-glucan 4-glucanohydrolase H(A16-M).
Related PDB2ayh
Related Swiss-protP23904
[12]
CommentsX-ray crystallography
PubMed ID7589539
JournalFEBS Lett
Year1995
Volume374
Pages221-4
AuthorsHahn M, Pons J, Planas A, Querol E, Heinemann U
TitleCrystal structure of Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase at 1.8 A resolution.
Related PDB1gbg
[13]
CommentsX-ray crystallography
PubMed ID7852389
JournalJ Biol Chem
Year1995
Volume270
Pages3081-8
AuthorsHahn M, Olsen O, Politz O, Borriss R, Heinemann U
TitleCrystal structure and site-directed mutagenesis of Bacillus macerans endo-1,3-1,4-beta-glucanase.
Related PDB1mac
[14]
PubMed ID8746732
JournalProtein Eng
Year1995
Volume8
Pages939-45
AuthorsPons J, Planas A, Querol E
TitleContribution of a disulfide bridge to the stability of 1,3-1,4-beta-D-glucan 4-glucanohydrolase from Bacillus licheniformis.
[15]
PubMed ID9374861
JournalBiochemistry
Year1997
Volume36
Pages13838-48
AuthorsMalet C, Planas A
TitleMechanism of Bacillus 1,3-1,4-beta-D-glucan 4-glucanohydrolases: kinetics and pH studies with 4-methylumbelliferyl beta-D-glucan oligosaccharides.
[16]
PubMed ID9698381
JournalBiochemistry
Year1998
Volume37
Pages11332-42
AuthorsViladot JL, de Ramon E, Durany O, Planas A
TitleProbing the mechanism of Bacillus 1,3-1,4-beta-D-glucan 4-glucanohydrolases by chemical rescue of inactive mutants at catalytically essential residues.
[17]
PubMed ID9799108
JournalEur J Biochem
Year1998
Volume257
Pages101-111
AuthorsKrah M, Misselwitz R, Politz O, Thomsen KK, Welfle H, Borriss R
TitleThe laminarinase from thermophilic eubacterium Rhodothermus marinus--conformation, stability, and identification of active site carboxylic residues by site-directed mutagenesis.
[18]
PubMed ID9862456
JournalFEBS Lett
Year1998
Volume440
Pages208-12
AuthorsMalet C, Planas A
TitleFrom beta-glucanase to beta-glucansynthase: glycosyl transfer to alpha-glycosyl fluorides catalyzed by a mutant endoglucanase lacking its catalytic nucleophile.
[19]
CommentsX-ray crystallography
PubMed ID9618460
JournalProc Natl Acad Sci U S A
Year1998
Volume95
Pages6613-8
AuthorsAy J, Gotz F, Borriss R, Heinemann U
TitleStructure and function of the Bacillus hybrid enzyme GluXyn-1: native-like jellyroll fold preserved after insertion of autonomous globular domain.
Related PDB1axk
[20]
CommentsX-ray crystallography
PubMed ID9489923
JournalProteins
Year1998
Volume30
Pages155-67
AuthorsAy J, Hahn M, Decanniere K, Piotukh K, Borriss R, Heinemann U
TitleCrystal structures and properties of de novo circularly permuted 1,3-1,4-beta-glucanases.
Related PDB1ajk,1ajo
[21]
PubMed ID10587432
JournalBiochemistry
Year1999
Volume38
Pages16092-104
AuthorsPiotukh K, Serra V, Borriss R, Planas A
TitleProtein-carbohydrate interactions defining substrate specificity in Bacillus 1,3-1,4-beta-D-glucan 4-glucanohydrolases as dissected by mutational analysis.
[22]
PubMed ID11150614
JournalBiochim Biophys Acta
Year2000
Volume1543
Pages361-382
AuthorsPlanas A
TitleBacterial 1,3-1,4-beta-glucanases: structure, function and protein engineering.
[23]
PubMed ID11526326
JournalActa Crystallogr D Biol Crystallogr
Year2001
Volume57
Pages1303-1306
AuthorsTsai LC, Shyur LF, Lin SS, Yuan HS
TitleCrystallization and preliminary X-ray diffraction analysis of the 1,3-1,4-beta-D-glucanase from Fibrobacter succinogenes.
[24]
PubMed ID11256951
JournalBiochem J
Year2001
Volume355
Pages79-86
AuthorsViladot JL, Canals F, Batllori X, Planas A
TitleLong-lived glycosyl-enzyme intermediate mimic produced by formate re-activation of a mutant endoglucanase lacking its catalytic nucleophile.
[25]
PubMed ID11279139
JournalJ Biol Chem
Year2001
Volume276
Pages17895-17901
AuthorsChen JL, Tsai LC, Wen TN, Tang JB, Yuan HS, Shyur LF
TitleDirected mutagenesis of apecific active site residues on Fibrobacter succinogenes 1,3-1,4-beta -D-glucanase significantly affects catalysis and enzyme structural stability.
[26]
PubMed ID11841232
JournalBiochemistry
Year2002
Volume41
Pages2388-2395
AuthorsAshida H, Maskos K, Li SC, Li YT
TitleCharacterization of a novel endo-beta-galactosidase specific for releasing the disaccharide GlcNAc alpha 1-->4Gal from glycoconjugates.
[27]
PubMed ID12093295
JournalBiochemistry
Year2002
Volume41
Pages8759-8766
AuthorsCheng HL, Tsai LC, Lin SS, Yuan HS, Yang NS, Lee SH, Shyur LF
TitleMutagenesis of Trp(54) and Trp(203) residues on Fibrobacter succinogenes 1,3-1,4-beta-D-glucanase significantly affects catalytic activities of the enzyme.
[28]
PubMed ID12842475
JournalJ Mol Biol
Year2003
Volume330
Pages607-20
AuthorsTsai LC, Shyur LF, Lee SH, Lin SS, Yuan HS
TitleCrystal structure of a natural circularly permuted jellyroll protein: 1,3-1,4-beta-D-glucanase from Fibrobacter succinogenes.

comments
This enzyme belongs to the glycosidase family-16. This is a retaining glycosidase enzyme, whose configuration of the sugar substrate will be retained after the catalytic reaction.
PDB structures, 1ajk, 1ajo, 1cpm and 2apn, are for the circularly permutated enzyme proteins, whilst that of 1axk is for the artificially fused enzyme with 1,4-beta-xylanase (EC 3.2.1.8; Swiss-prot, P18429).
According to the literature [15], [16] & [22], the catalytic reaction proceeds as follows:
(1) Glycosylation step:Glu105 (of 1byh) makes a nucleophilic attack on the C-1 atom of the polysaccharide substrate, forming a covalent glycosyl-enzyme intermediate through an oxocarbonium-like transition-state. At the same time, Glu109 assists this step as a general acid, to protonate the scissile glycosidic oxygen.
(2) Deglycosylation step:Glu102 acts as a general acid, to activate a water molecule, which then makes a nucleophilic attack on the C-1 atom of the covalent intermediate, resulting in the product release through the same transition state as in the glycosylation step (an oxocarbonium-like transition-state).

createdupdated
2004-07-122009-09-30
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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