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Information on EC 3.2.1.21 - beta-glucosidase and Organism(s) Zea mays and UniProt Accession P49235
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3.2.1.21 beta-glucosidaseIUBMB Comments
Wide specificity for beta-D-glucosides. Some examples also hydrolyse one or more of the following: beta-D-galactosides, alpha-L-arabinosides, beta-D-xylosides, beta-D-fucosides.
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Word Map
- 3.2.1.21
- cellobiose
- cellulase
- beta-galactosidase
- glycoside
- lysosomal
- alpha-glucosidase
- gaucher
- trichoderma
- aglycone
- endoglucanase
- glycosidases
-
cellulolytic
- almond
- xylanase
- reesei
- beta-xylosidase
-
saccharification
- alpha-mannosidase
- p-nitrophenyl
- alpha-galactosidase
-
lignocellulosic
- urease
- cellobiohydrolase
- avicel
-
cellulosic
- straw
- glucosylceramide
- cassava
- beta-n-acetylglucosaminidase
- xylan
- beta-d-glucopyranoside
- cmcase
- hemicellulose
-
microcrystalline
- beta-mannosidase
- arylamidase
- arbutin
- cellulomonas
-
transglucosylation
- stover
- alpha-l-fucosidase
- alpha-l-arabinofuranosidase
- cellotetraose
- bagasse
- azoreductase
- carboxymethylcellulase
- endo-beta-1,4-glucanase
- cellodextrins
- glucocerebroside
-
xylanolytic
- industry
- biofuel production
- medicine
- nutrition
- degradation
- analysis
- synthesis
- food industry
- molecular biology
- biotechnology
The taxonomic range for the selected organisms is: Zea mays
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
beta-glucosidase, linamarase, beta-glu, emulsin, bglu1, zm-p60.1, bgl1b, cel3a, novozyme 188, t-cell inhibitor, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
amygdalase
-
-
-
-
amygdalinase
-
-
-
-
arbutinase
-
-
-
-
aryl-beta-glucosidase
-
-
-
-
beta-1,6-glucosidase
-
-
-
-
beta-D-glucosidase
-
-
-
-
beta-D-glucoside glucohydrolase
-
-
-
-
beta-glucoside hydrolase
-
-
-
-
BGA
-
-
-
-
cellobiase
-
-
-
-
elaterase
-
-
-
-
emulsin
-
-
-
-
gentiobiase
-
-
-
-
limarase
-
-
-
-
Novozyme 188
-
-
-
-
p-nitrophenyl beta-glucosidase
-
-
-
-
primeverosidase
-
-
-
-
salicilinase
-
-
-
-
T-cell inhibitor
-
-
-
-
vicianase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
beta-D-glucoside glucohydrolase
Wide specificity for beta-D-glucosides. Some examples also hydrolyse one or more of the following: beta-D-galactosides, alpha-L-arabinosides, beta-D-xylosides, beta-D-fucosides.
CAS REGISTRY NUMBER
COMMENTARY
9001-22-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucose
-
-
-
?
2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one + H2O
2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one + beta-D-glucose
4-methylumbelliferyl beta-D-glucopyranoside + H2O
4-methylumbelliferone + beta-D-glucose
-
-
-
?
4-methylumbelliferyl-beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
dhurrin + H2O
(2S)-hydroxy(4-hydroxyphenyl)ethanenitrile + beta-D-glucose
-
-
-
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
low activity
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
low activity
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
relatively specific for aryl-beta-D-linked glucopyranoside substrates
-
?
2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one + H2O
2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one + beta-D-glucose
-
-
-
?
2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one + H2O
2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one + beta-D-glucose
i.e. DIMBOA-glucoside
-
-
?
additional information
?
-
Glu1 shows broad substrate specificity in vitro
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.76
2-nitrophenyl beta-D-glucopyranoside
pH 5.8, 37°C, mutant F198V/F205L/P377A
0.33
4-methylumbelliferyl beta-D-glucopyranoside
pH 5.8, 37°C, mutant F198V/F205L/P377A
0.76
4-methylumbelliferyl beta-D-glucopyranoside
pH 5.8, 37°C, mutant F466S/A467S
0.94
4-nitrophenyl beta-D-glucopyranoside
pH 5.8, 37°C, mutant F198V/F205L/P377A
0.076
Dhurrin
pH 5.8, 37°C, chimeric mutant (Chim21) bearing a C-terminal octapeptide (466-477) exchanged with the homologous octapeptide of Sorghum Dhr1
0.101
Dhurrin
pH 5.8, 37°C, chimeric mutant (Chim16) bearing a C-terminal octapeptide (466-477) exchanged with the homologous octapeptide of Sorghum Dhr1 (with an extra 22 amino acids substitution)
1.02
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
1.23
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
1.36
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
1.39
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
1.4
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
0.35
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
0.35
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
0.36
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
0.39
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
0.42
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
0.04
Dhurrin
-
pH 5.8, 37°C, mutant Chim23 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 492-508 of Zea mays)
0.09
Dhurrin
-
pH 5.8, 37°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
0.1
Dhurrin
-
pH 5.8, 37°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
0.12
Dhurrin
-
pH 5.8, 37°C, mutant Chim39 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 466-492 of Zea mays)
0.15
Dhurrin
-
pH 5.8, 37°C, mutant Chim17 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 462-508 of Zea mays)
0.18
Dhurrin
-
pH 5.8, 37°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
0.36
Dhurrin
-
pH 5.8, 37°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
19.1
2-nitrophenyl beta-D-glucopyranoside
pH 5.8, 37°C, mutant F198V/F205L/P377A
1.7
4-methylumbelliferyl beta-D-glucopyranoside
pH 5.8, 37°C, mutant F198V/F205L/P377A
87.2
4-methylumbelliferyl beta-D-glucopyranoside
pH 5.8, 37°C, mutant F466S/A467S
0.67
4-nitrophenyl beta-D-glucopyranoside
pH 5.8, 37°C, mutant F198V/F205L/P377A
1.32
Dhurrin
pH 5.8, 37°C, chimeric mutant (Chim21) bearing a C-terminal octapeptide (466-477) exchanged with the homologous octapeptide of Sorghum Dhr1
2.23
Dhurrin
pH 5.8, 37°C, chimeric mutant (Chim16) bearing a C-terminal octapeptide (466-477) exchanged with the homologous octapeptide of Sorghum Dhr1 (with an extra 22 amino acids substitution)
31.19
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
37.05
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
45.65
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
54.02
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
64.25
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
34.26
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
68.9
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
87.24
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
90.8
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
107.9
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
13.46
Dhurrin
-
pH 5.8, 37°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
18.68
Dhurrin
-
pH 5.8, 37°C, mutant Chim17 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 462-508 of Zea mays)
22.7
Dhurrin
-
pH 5.8, 37°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
23.41
Dhurrin
-
pH 5.8, 37°C, mutant Chim39 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 466-492 of Zea mays)
27.17
Dhurrin
-
pH 5.8, 37°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
31.83
Dhurrin
-
pH 5.8, 37°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
46.02
Dhurrin
-
pH 5.8, 37°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
22.43
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
26.46
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
43.91
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
44.75
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
47.24
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
97.88
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
196.4
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
216.4
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
242.6
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
276.7
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
26.1
Dhurrin
-
pH 5.8, 37°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
62.4
Dhurrin
-
pH 5.8, 37°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
124
Dhurrin
-
pH 5.8, 37°C, mutant Chim17 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 462-508 of Zea mays)
150
Dhurrin
-
pH 5.8, 37°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
195
Dhurrin
-
pH 5.8, 37°C, mutant Chim39 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 466-492 of Zea mays)
303.1
Dhurrin
-
pH 5.8, 37°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
494.8
Dhurrin
-
pH 5.8, 37°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
assay at 25°C, substrates: 2-nitrophenyl beta-D-glucopyranoside and 4-nitrophenyl beta-D-glucopyranoside
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). HGGL1_MAIZE
566
0
64237
Swiss-Prot
Chloroplast (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
enzyme specifically interacts with chimeric lectin beta-glucosidase aggregating factor resulting in high molecular weight complexes
additional information
-
enzyme specifically interacts with chimeric lectin beta-glucosidase aggregating factor resulting in high molecular weight complexes
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of mutant E191D,F198V is determined at 1.9 A resolution in complex with DIMBOA-glucoside
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D261N
the D261N substitution leads to a drastic decrease in relative efficiency of ZmGlu1 on all substrates tested, but little effect on the Km
E191D/F198V
inactive mutant, F198 substitution causes a rearrangement of residues F205, F466, and E464 involved in aglycone binding
F193A
increase in affinity for a small polar aglycone, deep decrease in kcat value. 7.8% of wild-type activity for substrate 4-nitrophenyl-beta-D-glucoside, 3% for substrate 4-methylumbelliferyl-beta-D-glucoside, respectively
F193A/F200K/W373K/F461L
almost complete loss of catalytic activity, extensive alterations in strucutre
F198V
mutant shows drastic effect on catalytic efficacy, kcat is reduced by 90% for hydrolysis of 4-methylumbelliferyl beta-D-glucopyranoside compared to wild-type. Mutant is unable to hydrolyze 4-nitrophenyl beta-D-glucopyranoside. Only negligible activity toward substrate 2-nitrophenyl beta-D-glucopyranoside compared to wild-type
F198V/F205L/P377A
mutant shows a drastic reduced relative efficacy for all test substrated due to a decreased turnover
F200K
1.1% of wild-type activity for substrate 4-nitrophenyl-beta-D-glucoside, 0.3% for substrate 4-methylumbelliferyl-beta-D-glucoside, respectively
F205L
Mutant shows similar relative efficacy compared to wild-type toward all substrates tested. Mutant shows no significant effect on hydrolysis of 4-nitrophenyl beta-D-glucopyranoside other than doubling the kcat value compared to wild-type
F461L
120% of wild-type activity for substrate 4-nitrophenyl-beta-D-glucoside, 119% for substrate 4-methylumbelliferyl-beta-D-glucoside, respectively
F466S
mutant exhibits a marked increase in relative efficiency in comparison to wild-type ZmGlu1 on all substrates tested (from 28 to 123%), because of increased substrate turnover. Mutant has little effect on dhurrin hydrolysis compared to wild-type (3% of relative efficacy compared to Sorghum Dhr1)
F466S/A467S
the A467S substitution in ZmGlu1 has no detectable effect on substrate specificity and catalytic efficiency in the case of 4-nitrophenyl beta-D-glucopyranoside or 2-nitrophenyl beta-D-glucopyranoside hydrolysis, and only a lower Km is obtained for 4-methylumbelliferyl beta-D-glucuronide compared to mutant F466S. Mutant has little effect on dhurrin hydrolysis compared to wild-type (3% of relative efficacy compared to Sorghum Dhr1)
K81E
mutant not able to bind chimeric lectin beta-glucosidase aggregating factor
M263F
mutant shows reduced relative efficacy by 40 to 50% on 4-nitrophenyl beta-D-glucopyranoside and 4-methylumbelliferyl beta-D-glucopyranoside whereas it shows an increase of about 60% relative efficacy on 2-nitrophenyl beta-D-glucopyranoside compared to wild-type
N481E
mutant with lowered affinity to cimeric lectin beta-glucosidase aggregating factor
P377A
P377A mutation leads to changes (decreases) in both kcat and Km for all substrated with no decrease in the overall relative efficiency
T82Y
mutant not able to bind chimeric lectin beta-glucosidase aggregating factor
W373K
large decrease in kcat value. 0.5% of wild-type activity for substrate 4-nitrophenyl-beta-D-glucoside, 0.04% for substrate 4-methylumbelliferyl-beta-D-glucoside, respectively
Y473F
kcat is increased by 110% to 450% depending on the substrate tested. Enhanced turnover is compensated by a slight increase in Km of this mutant giving a 40% to 250% (depending on the substrate tested) better relative efficacy over the wild-type enzyme. Mutation leads to a significant effect towards dhurrin hydrolysis (10% relative efficacy as compared to Sorghum Dhr1)
additional information
additional information
mutations in within residues S1 to T29 show no effect on binding of chimeric lectin beta-glucosidase aggregating factor
additional information
-
mutations in within residues S1 to T29 show no effect on binding of chimeric lectin beta-glucosidase aggregating factor
additional information
creation of chimeric mutants (Chim21 and Chim16) which are produced by reciprocal domain-swapping between ZmGlu1 and (Sorghum) SbDhr1: ZmGlu1 hydrolyzes dhurrin with a lower catalytic efficiency only when a C-terminal octapeptide 466-477 is exchanged with the homologous octapeptide of SorghumDhr1 (462-469). This peptide substitution leading to amino acid substitutions at four sites is found in Chim21 and Chim16 (with an extra 22 amino acids substitution) enables ZmGlu1 to hydrolyze dhurrin with less than 10% of the relative efficiency of SorghumDhr1 (7.4% for Chim21 and 9.5% for Chim16)
additional information
-
creation of chimeric mutants (Chim21 and Chim16) which are produced by reciprocal domain-swapping between ZmGlu1 and (Sorghum) SbDhr1: ZmGlu1 hydrolyzes dhurrin with a lower catalytic efficiency only when a C-terminal octapeptide 466-477 is exchanged with the homologous octapeptide of SorghumDhr1 (462-469). This peptide substitution leading to amino acid substitutions at four sites is found in Chim21 and Chim16 (with an extra 22 amino acids substitution) enables ZmGlu1 to hydrolyze dhurrin with less than 10% of the relative efficiency of SorghumDhr1 (7.4% for Chim21 and 9.5% for Chim16)
additional information
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to study the mechanism of substrate specificity further, eight chimeric beta-glucosidases are constructed by replacing peptide sequences within the C-terminal region of Zea mays Glu1 with the homologous peptide sequences of Sorghum Dhr1 or vice versa. Replacing the peptide 466FAGFTERY473 of Zea mays Glu1 with the homologous peptide 462SSGYTERF469 of Sorghum Dhr1 or replacing the peptide 481NNNCTRYMKE490 in Glu1 with the homologous peptide 477ENGCERTMKR486 of Dhr1 is sufficient to confer to Zea mays Glu1 the ability to hydrolyze dhurrin
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 45fold to homogeneity by ammonium sulfate fractionation, ion exchange chromatography, and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Feldwisch, J.; Vente, A.; Zettl, R.; Bako, L.; Campos, N.; Palme, K.
Characterization of two membrane-associated beta-glucosidases from maize (Zea mays L.) coleoptiles
Biochem. J.
302
15-21
1994
Zea mays
Verdoucq, L.; Moriniere, J.; Bevan, D.R.; Esen, A.; Vasella, A.; Henrissat, B.; Czjze, M.
Structural determinants of substrate specificity in family 1 beta-glucosidases: novel insights from the crystal structure of sorghum dhurrinase-1, a plant beta-glucosidase with strict specificity, in complex with its natural substrate
J. Biol. Chem.
279
31796-31803
2004
Sorghum bicolor, Zea mays (P49235), Zea mays
Han, Y.; Chen, H.
Characterization of beta-glucosidase from corn stover and its application in simultaneous saccharification and fermentation
Biores. Technol.
99
6081-6087
2008
Zea mays
Yu, H.Y.; Kittur, F.S.; Bevan, D.R.; Esen, A.
Lysine-81 and threonine-82 on maize beta-glucosidase isozyme Glu1 are the key amino acids involved in beta-glucosidase aggregating factor binding (dagger)
Biochemistry
48
2924-2932
2009
Zea mays (P49235), Zea mays
Dopitova, R.; Mazura, P.; Janda, L.; Chaloupkova, R.; Jerabek, P.; Damborsky, J.; Filipi, T.; Kiran, N.S.; Brzobohaty, B.
Functional analysis of the aglycone-binding site of the maize beta-glucosidase Zm-p60.1
FEBS J.
275
6123-6135
2008
Zea mays (P49235), Zea mays
Cicek, M.; Blanchard, D.; Bevan, D.R.; Esen, A.
The aglycone specificity-determining sites are different in 2, 4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA)-glucosidase (Maize beta -glucosidase) and dhurrinase (Sorghum beta -glucosidase)
J. Biol. Chem.
275
20002-20011
2000
Sorghum bicolor, Zea mays
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