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Information on EC 3.2.1.73 - licheninase and Organism(s) Hordeum vulgare and UniProt Accession P12257

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EC Tree
     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.73 licheninase
IUBMB Comments
Acts on lichenin and cereal beta-D-glucans, but not on beta-D-glucans containing only 1,3- or 1,4-bonds.
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This record set is specific for:
Hordeum vulgare
UNIPROT: P12257
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The taxonomic range for the selected organisms is: Hordeum vulgare
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
endoglucanase, plica, glu-1, glu-3, endo-beta-glucanase, 1,3-1,4-beta-glucanase, 1,3-1,4-beta-d-glucanase, bglc8h, af-egl7, xyniii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lichenase-2
-
(1->3,1->4)-beta-glucanase isoenzyme EII
-
-
-
-
1,3-1,4-beta-D-glucan 4-glucanohydrolase
-
-
-
-
1,3-1,4-beta-D-glucan glucanohydrolase
-
-
-
-
1,3;1,4-beta-glucan 4-glucanohydrolase
-
-
-
-
1,3;1,4-beta-glucan endohydrolase
-
-
-
-
beta-(1--> 3), (1--> 4)-D-glucan 4-glucanohydrolase
-
-
-
-
beta-glucanase
-
-
endo-beta-1,3-1,4 glucanase
-
-
-
-
laminarinase
-
-
-
-
Lichenase
-
-
-
-
Mixed linkage beta-glucanase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
(1->3)-(1->4)-beta-D-glucan 4-glucanohydrolase
Acts on lichenin and cereal beta-D-glucans, but not on beta-D-glucans containing only 1,3- or 1,4-bonds.
CAS REGISTRY NUMBER
COMMENTARY hide
37288-51-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(1-3,1-4)-beta-D-glucan + H2O
?
show the reaction diagram
-
i.e. barley (1-3,1-4)-beta-glucan
-
-
?
barley beta-D-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
beta-(1-3),(1-4)-D-glucan + H2O
beta-D-glucose + ?
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
epoxyalkyl cellobiosides
-
irreversible active-site directed inactivation, stereospecific requirements for inhibition
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14.5
-
37°C, pH 5.0
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
-
wild type, mutant H300P
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
isoenzyme II is synthesized exclusively in the aleurone layer, isoenzyme III is detected in scutellum and aleurone layer
Manually annotated by BRENDA team
-
isoenzyme I is synthesized predominantly in the scutellum, isoenzyme III is detected in scutellum and aleurone layer
Manually annotated by BRENDA team
-
transfer from antural light/dark cycle into darkness induces eisozyme EI
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
overexpression of barley (1->3,1->4)-beta-glucanase isoenzyme EII under the control of a promoter of barley D-Hordein gene Hor3-1 in barley cultivar Golden Promise. The T2 generation of transgenic lines shows increased activity of glucanase in grains. Total beta-glucan content is reduced by more than 95.73% in transgenic grains compared with the wild-type control. Overexpression leads to an increase in 1000-grain weight, which might be due to elevated amounts of starch in the grain
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GUB2_HORVU
312
0
32774
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27700
-
enzyme I, ultracentrifugation
28000
30000
-
x * 30000, SDS-PAGE
32085
-
x * 32085, calculation from nucleotide sequence
33500
-
x * 33500, SDS-PAGE, recombinant enzyme with His-tag
33800
-
enzyme II, ultracentrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
enzyme I contains 0.7% carbohydrate of which three residues are probably N-acetylglucosamine, enzyme II contains 3.6% carbohydrate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A79P
-
decrease in thermal stability
F85Y
-
decrease in thermal stability
G44R
-
decrease in thermal stability
H300P
-
increase in thermal stability
K23R
-
decrease in thermal stability
M298K
-
thermal stabiltiy similar to wild type
N290H
-
slight increase in thermal stability
additional information
-
protein-engineered, thermostable (1,3-1,4)-beta-glucanase: the codons for hybrid H(A12-M)DELTAY13 are modified to match those of the gene encoding barley (1,3-1,4)-beta-glucanase isoenzyme EII
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 5
-
25°C, 72-96 h, stable
171531
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
pH 5.5, 10 min, stable
44.5
-
15 min, 50% of activity, mutant G44R
46
-
15 min, 50% of activity, mutant K23R
46.1
-
15 min, 50% of activity, mutant A79P
46.2
-
15 min, 50% of activity, mutant F85Y
47.5
-
15 min, 50% of activity, wild type
47.9
-
15 min, 50% of activity, mutant M298K, mutant T17D
48.2
-
15 min, 50% of activity, mutant N290H
51.2
-
15 min, 50% of activity, mutant H300P
60
-
pH 5.5, 10 min, complete loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, stable for 12 months
-
4°C, 50 mM sodium phosphate, pH 7.8, 300 mM sodium chloride, stable for several weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
expression in Escherichia coli, isolation and characterization of the gene
-
transgenic barley expressing a protein-engineered, thermostable (1,3-1,4)-beta-glucanase during germination
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
overexpression of barley (1->3,1->4)-beta-glucanase isoenzyme EII under the control of a promoter of barley D-Hordein gene Hor3-1 in barley cultivar Golden Promise. The T2 generation of transgenic lines shows increased activity of glucanase in grains. Total beta-glucan content is reduced by more than 95.73% in transgenic grains compared with the wild-type control. Overexpression leads to an increase in 1000-grain weight, which might be due to elevated amounts of starch in the grain
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Stuart, I.M.; Loi, L.; Fincher, G.B.
Development of (1->3,1->4)-beta-D-glucan endohydrolase isoenzymes in isolated scutella and aleurone layers of barley (Hordeum vulgare)
Plant Physiol.
80
310-314
1986
Hordeum vulgare
Manually annotated by BRENDA team
Yamashita, H.; Hayase, F.; Kato, H.
beta-Glucanases in malt that form insoluble material
Agric. Biol. Chem.
49
1313-1320
1985
Hordeum vulgare
-
Manually annotated by BRENDA team
Woodward, J.R.; Fincher, G.B.
Purification and chemical properties of two 1,3;1,4-beta-glucan endohydrolases from germinating barley
Eur. J. Biochem.
121
663-669
1982
Hordeum vulgare
Manually annotated by BRENDA team
Jensen, L.G.; Olsen, O.; Kops, O.; Wolf, N.; Thomsen, K.K.; von Wettstein, D.
Transgenic barley expressing a protein-engineered, thermostable (1,3-1,4)-beta-glucanase during germination
Proc. Natl. Acad. Sci. USA
93
3487-3491
1996
Hordeum vulgare
Manually annotated by BRENDA team
Hoj, P.B.; Rodriguez, E.B.; Iser, J.R.; Stick, R.V.; Stone, B.A.
Active site-directed inhibition by optically pure epoxyalkyl cellobiosides reveals differences in active site geometry of two 1,3-1,4-beta-D-glucan 4-glucanohydrolase
J. Biol. Chem.
266
11628-11631
1991
Bacillus subtilis, Hordeum vulgare
Manually annotated by BRENDA team
Litts, J.C.; Simmons, C.R.; Karrer, E.E.; Huang, N.; Rodriguez, R.L.
The isolation and characterization of a barley 1,3-1,4-beta-glucanase gene
Eur. J. Biochem.
194
831-838
1990
Hordeum vulgare
Manually annotated by BRENDA team
Roulin, S.; Buchala, A.J.; Fincher, G.B.
Induction of (1-3,1-4)-beta-D-glucan hydrolases in leaves of dark-incubated barley seedlings
Planta
215
51-59
2002
Hordeum vulgare
Manually annotated by BRENDA team
Stewart, R.J.; Varghese, J.N.; Garrett, T.P.J.; Hoj, P.B.; Fincher, G.B.
Mutant barley (1-3,1-4)-beta-glucan endohydrolases with enhanced thermostability
Protein Eng.
14
245-253
2001
Hordeum vulgare
Manually annotated by BRENDA team
Gianinetti, A.; Ferrari, B.; Frigeri, P.; Stanca, A.M.
In vivo modeling of beta-glucan degradation in contrasting barley (Hordeum vulgare L.) genotypes
J. Agric. Food Chem.
55
3158-3166
2007
Hordeum vulgare
Manually annotated by BRENDA team
Han, N.; Na, C.; Chai, Y.; Chen, J.; Zhang, Z.; Bai, B.; Bian, H.; Zhang, Y.; Zhu, M.
Over-expression of (1,3;1,4)-beta-D-glucanase isoenzyme EII gene results in decreased (1,3;1,4)-beta-D-glucan content and increased starch level in barley grains
J. Sci. Food Agric.
97
122-127
2017
Hordeum vulgare (P12257)
Manually annotated by BRENDA team