Information on EC 3.2.1.2 - beta-amylase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
3.2.1.2
-
RECOMMENDED NAME
GeneOntology No.
beta-amylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
show the reaction diagram
multichain type mechanism
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
show the reaction diagram
catalytic mechanism
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
show the reaction diagram
catalytic mechanism, reaction mechanism
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
show the reaction diagram
mechanism
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
show the reaction diagram
acts on starch, glycogen and related polysaccharides and oligosaccharides producing beta-maltose by an inversion, the term beta relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolysed
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
show the reaction diagram
mode of action of the exo-amylase
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
show the reaction diagram
Glu367 is important in catalysis, the plant enzyme shows a reaction mechanism different from the bacterial enzyme, overview
P36924
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
show the reaction diagram
active site structure, carbohydrate binding subsites, role of a conformational change of the inner loop in the catalytic mechanism, T342 is involved, overview
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
show the reaction diagram
catalytic mechanism
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
show the reaction diagram
roles of Glu186 and Glu380 as general acid and general base catalyst in the catalytic reaction, substrate binding and reaction mechanism
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
show the reaction diagram
general acid-base catalytic reaction mechanism
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
show the reaction diagram
roles of Glu186 and Glu380 as general acid and general base catalyst in the catalytic reaction, reaction mechanism involving residue T342
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
show the reaction diagram
mode of action of the exo-amylase
Syncephalastrum racemosum RR96
-
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
show the reaction diagram
acts on starch, glycogen and related polysaccharides and oligosaccharides producing beta-maltose by an inversion, the term beta relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolysed
Xanthophyllomyces dendrorhous CECT1690
-
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
exohydrolysis
-
PATHWAY
KEGG Link
MetaCyc Link
Metabolic pathways
-
Starch and sucrose metabolism
-
starch degradation I
-
starch degradation II
-
SYSTEMATIC NAME
IUBMB Comments
4-alpha-D-glucan maltohydrolase
Acts on starch, glycogen and related polysaccharides and oligosaccharides producing beta-maltose by an inversion. The term 'beta'' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolysed.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
(1-4)-alpha-D-glucan maltohydrolase
-
-
-
-
1,4-alpha-D-glucan malto-hydrolase
-
-
1,4-alpha-D-glucan maltohydrolase
-
-
-
-
amylase, beta-
-
-
-
-
ARATH
O23553
-
BAM-1
-
chloroplastic
BAM-2
-
chloroplastic
BAM-3
-
chloroplastic
BAM1
D0VBH4
isozyme
BAM3
-
catalytically active beta-amylase
BAM4
-
catalytically inactive beta-amylase
beta amylase
-
-
-
-
beta-amylase
-
-
beta-amylase
-
-
beta-amylase
-
-
beta-amylase
-
-
beta-amylase
P10537
-
beta-amylase
-
-
beta-amylase
Q8U2G5
-
beta-amylase
Xanthophyllomyces dendrorhous CECT1690
-
-
-
beta-amylase 1
Q9LIR6
-
beta-amylase I
Q9AVJ8, Q9FUK6
-
beta-amylase1
-
-
beta-amylase2
-
-
beta-amylase8
O23553
-
Bmy1
Q9AVJ8, Q9FUK6
-
Cs-COR018
-
-
CT-BMY
O23553
-
PF0870
Q8U2G5
gene name
saccharogen amylase
-
-
-
-
saccharogenamylase
-
-
-
-
SBA
-
soybean beta-amylase
Sd1
-
one of three allelic forms of Hordeum beta-amylase
Sd2H
-
one of three allelic forms of Hordeum beta-amylase
Sd2L
-
one of three allelic forms of Hordeum beta-amylase
TR-BAMY
Q9LIR6
-
type I beta-amylase
-
-
type II beta-amylase
-
-
glycogenase
-
-
-
-
additional information
-
BAM-4 is chloroplastic, expressed in Escherichia coli with no beta-amylase activity, probably lost its catalytic capacity during evolution
additional information
-
belongs to family 14
additional information
-
member of family 14 of the sequence-based classification of glycoside hydrolases
CAS REGISTRY NUMBER
COMMENTARY
9000-91-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
ecotype Col-0
-
-
Manually annotated by BRENDA team
ecotype Columbia
-
-
Manually annotated by BRENDA team
gene At3g23920/F14O13_11, isozyme TR-BAMY; contains six extrachloroplastic isozymes, and three plastid-targeted isozymes
SwissProt
Manually annotated by BRENDA team
gene At4g170990, isozyme CT-BAMY; contains six extrachlorplastic isozymes, and three plastid-targeted isozymes
SwissProt
Manually annotated by BRENDA team
gene dl4575c or At4g170990, putative beta-amylase; ecotype Columbia, gene dl4575c or At4g170990
SwissProt
Manually annotated by BRENDA team
several isozymes
-
-
Manually annotated by BRENDA team
hyperproductive strain BQ10-S1 SpoIII
-
-
Manually annotated by BRENDA team
strains BQ10-S1 and BQ10-S1 SpoII
-
-
Manually annotated by BRENDA team
strains: ATCC 8145, ATCC 9524, ATCC 9634, ATCC 10876, ATCC 11778, ATCC 11950, ATCC 19637, IP 1010, IP 5227, IP 53137, NRRL 569, PZH 1011
-
-
Manually annotated by BRENDA team
var. mycoides
Uniprot
Manually annotated by BRENDA team
Bacillus circulans NCIMB 11033
-
UniProt
Manually annotated by BRENDA team
precursor; strain DSM319
SwissProt
Manually annotated by BRENDA team
sensu strictu, NCIB 7581
-
-
Manually annotated by BRENDA team
strains: IP 5261, NCIB 8291, NCIB 8508, PZH 53, PZH 493
-
-
Manually annotated by BRENDA team
Bacillus megaterium B6
strain B6
-
-
Manually annotated by BRENDA team
Bacillus megaterium DSM319
precursor; strain DSM319
SwissProt
Manually annotated by BRENDA team
hedge bindweed, collected in Leuven in winter
SwissProt
Manually annotated by BRENDA team
pearl millet, several cultivars, overview
-
-
Manually annotated by BRENDA team
tuberous-rooted chervil
-
-
Manually annotated by BRENDA team
Debaryomyces sp.
-
-
-
Manually annotated by BRENDA team
Dioscorea batatus
cultivar ichoimo
-
-
Manually annotated by BRENDA team
strain 45
-
-
Manually annotated by BRENDA team
strains 45 and MNU82
-
-
Manually annotated by BRENDA team
Emericella nidulans 45
strain 45
-
-
Manually annotated by BRENDA team
7 isoenzymes: 1', 1, 2, 3, 4, 5 and 6
-
-
Manually annotated by BRENDA team
isolated from soil sample from a salt lake obtained from Yuncheng, China
-
-
Manually annotated by BRENDA team
isolated from soil sample from a salt lake obtained from Yuncheng, China
-
-
Manually annotated by BRENDA team
17 Hordeum species, some with several suspecies, overview
-
-
Manually annotated by BRENDA team
3 allelic forms: Sd1, Sd2H and Sd2L, amino acid differences between the 3 forms, wild barley subsp. spontaneum NPGS PI29689, var. Haruna Nijo, Adorra and Hiproly
-
-
Manually annotated by BRENDA team
cvs. Morex and Steptoe, 2 isozymes beta-amylase1 and beta-amylase2, i.e. Bmy1 and Bmy2
-
-
Manually annotated by BRENDA team
fragment; analysis of coding sequence diversity in the Bmy1 gene on chromosome 4H
SwissProt
Manually annotated by BRENDA team
var. Franklin: Sd1, var. Schooner: Sd2L
Uniprot
Manually annotated by BRENDA team
variety A 7130
-
-
Manually annotated by BRENDA team
variety Triumph and abscisic acid-sensitive barley mutant TL43
-
-
Manually annotated by BRENDA team
varieties Tainung No. 57 and Chailai
-
-
Manually annotated by BRENDA team
Linn. cv. Keitt
-
-
Manually annotated by BRENDA team
L. cv. sonora
-
-
Manually annotated by BRENDA team
cv. Nanicao
SwissProt
Manually annotated by BRENDA team
gene BAC83770, putative beta-amylase, japonica group; var. japonica and indica, different cultivars, 98 backcross inbred lines from japonica x indica, i.e. Nipponbare x Kasalath, cross, overview
SwissProt
Manually annotated by BRENDA team
gene Bac83773, putative beta-amylase, japonica group; var. japonica and indica, different cultivars, 98 backcross inbred lines from japonica x indica, i.e. Nipponbare x Kasalath, cross, overview
SwissProt
Manually annotated by BRENDA team
L. var. Kimmaze
-
-
Manually annotated by BRENDA team
L. var. Shinsetsu
-
-
Manually annotated by BRENDA team
strains: NCIB 4747, NCIB 7575, NCIB 8158, NCIB 8524. The most potential beta-amylase producer is the strain NCIB 8524
-
-
Manually annotated by BRENDA team
Paenibacillus polymyxa No. 26-1
No. 26-1
-
-
Manually annotated by BRENDA team
Paenibacillus polymyxa No. 72
No. 72
-
-
Manually annotated by BRENDA team
Sorghum sp.
50 varieties
-
-
Manually annotated by BRENDA team
Sorghum sp.
cultivar ICSV 111
-
-
Manually annotated by BRENDA team
Syncephalastrum racemosum RR96
strain RR96
-
-
Manually annotated by BRENDA team
cv. Yangmai 158, isozymes type I and type II
-
-
Manually annotated by BRENDA team
strain CECT1690, the perfect state of Phaffia rhodozyma
-
-
Manually annotated by BRENDA team
Xanthophyllomyces dendrorhous CECT1690
strain CECT1690, the perfect state of Phaffia rhodozyma
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl alpha-D-galactoside + H2O
4-nitrophenol + D-galactose
show the reaction diagram
-, Q8U2G5
-
-
-
?
4-nitrophenyl alpha-maltopyranoside + H2O
4-nitrophenol + alpha-maltopyranose
show the reaction diagram
-, Q8U2G5
-
-
-
?
4-nitrophenyl maltopentaose + H2O
4-nitrophenol + maltopentaose
show the reaction diagram
O23553, Q9LIR6
-
-
-
?
4-nitrophenyl-maltoheptaoside + H2O
?
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-maltopentaoside + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-glucan + H2O
?
show the reaction diagram
Q3S4X4
-
-
-
?
amylopectin + H2O
maltose
show the reaction diagram
-
-
-
-
?
amylopectin + H2O
maltose
show the reaction diagram
P36924
-
-
-
?
amylopectin + H2O
maltose
show the reaction diagram
Sorghum sp.
-
from starch, preferred substrate
-
-
?
amylopectin + H2O
maltose
show the reaction diagram
-
from potato
-
-
?
amylopectin + H2O
maltose
show the reaction diagram
P36924
from potato
-
-
?
amylopectin + H2O
?
show the reaction diagram
-
114.6% of the activity with amylose, soluble starch, amylose and amylopectin are the most suitable substrates, exo-hydrolase that releases beta-maltose from the non-reducing end of alpha-1,4-linked poly- and oligoglucans until the first alpha-1,6-branching point along the substrate molecule is encountered
-
-
?
amylopectin + H2O
?
show the reaction diagram
-
88% of the activity with starch
-
-
?
amylopectin + H2O
?
show the reaction diagram
P10538
from potato, active site structure, Glu-186 and Glu-380 play important roles as general acid and base catalyst
-
-
?
amylopectin + H2O
?
show the reaction diagram
Bacillus megaterium B6
-
88% of the activity with starch
-
-
?
amylopectin + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
amylopectin + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
amylopectin + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
amylopectin + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
amylopectin + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
amylopectin + H2O
beta-maltose
show the reaction diagram
-
-
-
?
amylopectin + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
amylopectin + H2O
beta-maltose
show the reaction diagram
-
-
-
?
amylopectin + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
amylopectin + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
amylopectin + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
amylopectin + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
amylopectin + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
amylopectin + H2O
beta-maltose
show the reaction diagram
-
-
and limit dextrin
?
amylopectin + H2O
beta-maltose
show the reaction diagram
Paenibacillus polymyxa No. 26-1
-
-
-
-
?
amylopectin + H2O
maltose + ?
show the reaction diagram
-, Q9FQ07
catalyzes the release of maltose residues, amylopectin and starch are better substrates than amylose
-
-
?
amylose + H2O
?
show the reaction diagram
-
79% of the activity with starch
-
-
?
amylose + H2O
?
show the reaction diagram
-
DPn is 16
-
-
?
amylose + H2O
?
show the reaction diagram
-
EX-I, soluble starch, amylose and amylopectin are the most suitable substrates, exo-hydrolase that releases beta-maltose from the non-reducing end of alpha-1,4-linked poly- and oligoglucans until the first alpha-1,6-branching point along the substrate molecule is encountered
-
-
?
amylose + H2O
?
show the reaction diagram
Bacillus megaterium B6
-
79% of the activity with starch
-
-
?
amylose + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
amylose + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
amylose + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
amylose + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
amylose + H2O
beta-maltose
show the reaction diagram
-
-
-
?
amylose + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
amylose + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
amylose + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
amylose + H2O
beta-maltose
show the reaction diagram
-
-
-
?
amylose + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
amylose + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
amylose + H2O
beta-maltose
show the reaction diagram
-
-
-
?
amylose + H2O
beta-maltose
show the reaction diagram
-
partly oxidized amylose
-
-
?
amylose + H2O
beta-maltose
show the reaction diagram
-
DP = 17
-
-
?
amylose + H2O
beta-maltose
show the reaction diagram
Paenibacillus polymyxa No. 26-1
-
-
-
-
?
amylose + H2O
maltose + ?
show the reaction diagram
-, Q9FQ07
catalyzes the release of maltose residues, less good substrate than starch and amylopectin
-
-
?
amylose + H2O
maltose
show the reaction diagram
Sorghum sp.
-
from starch
-
-
?
dextrin + H2O
?
show the reaction diagram
-
-
-
-
?
dextrin + H2O
?
show the reaction diagram
Bacillus megaterium, Bacillus megaterium B6
-
13% of the activity with starch
-
-
?
glycogen + H2O
?
show the reaction diagram
-
49.4% of the activity with amylose
-
-
?
glycogen + H2O
?
show the reaction diagram
-, Q8U2G5
the enzyme is specific for short alpha-glucans. Similar responses to maltose, glycogen, and starch but not to pullulan
-
-
?
glycogen + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
glycogen + H2O
beta-maltose
show the reaction diagram
-
-
-
?
glycogen + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
glycogen + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
glycogen + H2O
beta-maltose
show the reaction diagram
-
-
and limit dextrin
?
glycogen + H2O
beta-maltose
show the reaction diagram
-
from oyster
-
-
?
glycogen + H2O
beta-maltose
show the reaction diagram
-
type III and type VIII
-
-
?
maltal + H2O
2-deoxymaltose
show the reaction diagram
-
-
-
?
maltodextrin + H2O
maltose
show the reaction diagram
-
maltodextrins with chain length from 9 to 198 glucose residues
and very small amounts of glucose and maltotriose
?
maltoheptaose + H2O
?
show the reaction diagram
-
-
-
-
?
maltoheptaose + H2O
?
show the reaction diagram
-
-
-
-
?
maltoheptaose + H2O
?
show the reaction diagram
-
-
-
-
?
maltoheptaose + H2O
?
show the reaction diagram
-
34.6% of the activity with amylose
-
-
?
maltoheptaose + H2O
maltose
show the reaction diagram
-
the exo-type enzyme can catalyze the successive liberation of beta-maltose from the nonreducing ends of alpha-1,4-linked glucopyranosyl polymers. A phenomenon called multiple or repetitive attack is observed where the enzyme releases several maltose molecules in a single enzyme-substrate complex. The multiple attack action needs the force of enzyme sliding on the substrate. In addition, it is important for the multiple attack that the enzyme and substrate have the characteristics of a stable productive substrate-enzyme complex through a hydrogen bond between the nonreducing end of the substrate and the carboxyl residue of the enzyme
-
-
?
maltohexaose + H2O
?
show the reaction diagram
-
-
-
-
?
maltohexaose + H2O
?
show the reaction diagram
-
-
-
-
?
maltohexaose + H2O
?
show the reaction diagram
-
23.3% of the activity with amylose
-
-
?
maltooligosaccharide + H2O
?
show the reaction diagram
-
beta-amylase hydrolyzes maltooligosaccharides more readily as their degree of polymerization increases, this being strongest for maltooligosaccharides larger than 13 glucose residues and very weakly for maltotriose, exo-hydrolase that releases beta-maltose from the non-reducing end of alpha-1,4-linked poly- and oligoglucans until the first alpha-1,6-branching point along the substrate molecule is encountered
-
-
?
maltopentaose + H2O
?
show the reaction diagram
-
-
-
-
?
maltopentaose + H2O
?
show the reaction diagram
-
-
-
-
?
maltopentaose + H2O
?
show the reaction diagram
-
13.8% of the activity with amylose
-
-
?
maltopentaose + H2O
?
show the reaction diagram
-
beta-amylase is an exo-enzyme that catalyzes the hydrolysis of the alpha-1,4-glucosidic linkage of the substrate liberating beta-maltose from the non-reducing end, Glu-172 and Glu-367 are catalytic residues, binding mode of substrate, substrate recognition mechanism, enzyme structure
-
-
?
maltopentaose + H2O
?
show the reaction diagram
-
beta-amylase is an inverting enzyme that hydrolyzes the alpha-1,4-glucosidic linkage of the substrate liberating beta-maltose from the non-reducing end, catalytic mechanism, Glu-172 acts as general acid, Glu-367 acts as general base
-
-
?
maltopentaose + H2O
?
show the reaction diagram
-
binding mode of substrate in the active site
-
-
?
maltopentaose + H2O
?
show the reaction diagram
P36924
hydrolyzes the alpha-1,4-glucosidic linkage liberating beta-maltose from the non-reducing end of substrate, good substrate, mode of binding in the active site, catalytic mechanism, enzyme/domain structure
-
-
?
maltopentaose + H2O
maltose
show the reaction diagram
-
substrate/product binding structure, sugar subsite conformations, overview
-
-
?
maltopentose + H2O
?
show the reaction diagram
Xanthophyllomyces dendrorhous, Xanthophyllomyces dendrorhous CECT1690
-
40% of the activity with starch, exo-acting enzyme, no production of glucose
-
-
?
maltose + H2O
?
show the reaction diagram
-, Q8U2G5
the enzyme is specific for short alpha-glucans. Similar responses to maltose, glycogen, and starch but not to pullulan
-
-
?
maltotetraose + H2O
?
show the reaction diagram
-
-
-
-
?
maltotetraose + H2O
?
show the reaction diagram
-
-
-
-
?
maltotetraose + H2O
?
show the reaction diagram
-
37% of the activity with starch, exo-acting enzyme, no production of glucose
-
-
?
maltotetraose + H2O
?
show the reaction diagram
-
7.6% of the activity with amylose
-
-
?
maltotetraose + H2O
?
show the reaction diagram
Xanthophyllomyces dendrorhous CECT1690
-
37% of the activity with starch, exo-acting enzyme, no production of glucose
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + glucose
show the reaction diagram
-
-
-
-
?
p-nitrophenylmaltopentaoside + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrophenylmaltopentaoside + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrophenylmaltopentaoside + H2O
?
show the reaction diagram
P16098
catalyzes the release of maltose
-
-
?
p-nitrophenylmaltopentaoside + H2O
?
show the reaction diagram
-
catalyzes the release of maltose
-
-
?
p-nitrophenylmaltopentaoside + H2O
p-nitrophenol + maltopentaose
show the reaction diagram
-, Q9FQ07
catalyzes the release of p-nitrophenol, specific substrate
-
-
?
pullulan + H2O
?
show the reaction diagram
-
-
-
-
?
soluble starch + H2O
?
show the reaction diagram
-
-
-
-
?
soluble starch + H2O
?
show the reaction diagram
-
starch granules from various sources
-
-
?
starch + H2O
?
show the reaction diagram
-
beta-amylase should be a key enzyme in starch degradation during the germination of millet seeds, enzyme activity increases during days 1-4 of germination, 106.9% of the activity with amylose, soluble starch, amylose and amylopectin are the most suitable substrates, some activity against native starch, exo-hydrolase that releases beta-maltose from the non-reducing end of alpha-1,4-linked poly- and oligoglucans until the first alpha-1,6-branching point along the substrate molecule is encountered
-
-
?
starch + H2O
?
show the reaction diagram
P10538
active site structure, Glu-186 and Glu-380 play important roles as general acid and base catalyst, catalyzes the liberation of beta-anomeric maltose from the non-reducing ends
-
-
?
starch + H2O
?
show the reaction diagram
-
beta-amylase hydrolyzes alpha-1,4-linkage, raw starch granules from potato, wheat, rice and corn, with the granules from rice being the best substrate, beta-amylase attacks very slowly on the starch granules, hydrolyzes corn granules efficiently at 45C
-
-
?
starch + H2O
?
show the reaction diagram
-
beta-amylase hydrolyzes alpha-1,4-linkage, raw starch granules from potato, wheat, rice and corn, with the granules from rice being the best substrate, no efficient hydrolysis of raw starch granules, very slow enzymic attack
-
-
?
starch + H2O
?
show the reaction diagram
-
beta-amylase is an exo-enzyme that catalyzes the hydrolysis of the alpha-1,4-glucosidic linkage of the substrate liberating beta-maltose from the non-reducing end, Glu-172 and Glu-367 are catalytic residues, substrate recognition mechanism, enzyme structure
-
-
?
starch + H2O
?
show the reaction diagram
-
beta-amylase is an inverting enzyme that hydrolyzes the alpha-1,4-glucosidic linkage of the substrate liberating beta-maltose from the non-reducing end, catalytic mechanism, Glu-172 acts as general acid, Glu-367 acts as general base
-
-
?
starch + H2O
?
show the reaction diagram
-
catalyzes the hydrolysis of alpha-1,4-glucosidic linkages of soluble starch, and liberates beta-anomeric maltose from the nonreducing ends, exo-acting enzyme, composed of two functional domains, a catalytic domain: domains A and B, and starch-binding domain: domain C, beta-amylase has three carbohydrate-binding sites aside from the active site: two in domain B named Site2 and Site3, one in domain C named Site1, roles of these sites in the catalytic reaction and raw starch-binding, beta-amylase hardly hydrolyzes raw starch from wheat, corn, potato or sweet potato, but binds to it strongly
-
-
?
starch + H2O
?
show the reaction diagram
-
catalyzes the release of maltose from soluble starch, three-dimensional structures of Sd2L and V233A mutant of Sd1
-
-
?
starch + H2O
?
show the reaction diagram
P16098
from potato, catalyzes the release of maltose from the non-reducing ends of starch, three-dimensional structure of Sd2L
-
-
?
starch + H2O
?
show the reaction diagram
-
highest activity, exo-acting enzyme, no production of glucose
-
-
?
starch + H2O
?
show the reaction diagram
P36924
hydrolyzes the alpha-1,4-glucosidic linkage liberating beta-maltose from the non-reducing end of substrate, enzyme/domain structure, starch binding site in domain C, catalytic mechanism
-
-
?
starch + H2O
?
show the reaction diagram
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran, the enzyme from strain MNU82 utilizes raw and cooked starch
-
-
?
starch + H2O
?
show the reaction diagram
O23553, Q9LIR6
in vitro breakdown of semicrystalline starch particles by beta-amylases increases significantly if they act together with glucan, water dikinase
-
-
?
starch + H2O
?
show the reaction diagram
-, Q8U2G5
the enzyme is specific for short alpha-glucans. Similar responses to maltose, glycogen, and starch but not to pullulan
-
-
?
starch + H2O
?
show the reaction diagram
Xanthophyllomyces dendrorhous CECT1690
-
highest activity, exo-acting enzyme, no production of glucose
-
-
?
starch + H2O
?
show the reaction diagram
Syncephalastrum racemosum RR96
-
-, starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
maltose
show the reaction diagram
-
-
-
?
starch + H2O
maltose
show the reaction diagram
-
-
-
?
starch + H2O
maltose
show the reaction diagram
-
-
-
-
?
starch + H2O
maltose
show the reaction diagram
-
-
-
-
?
starch + H2O
maltose
show the reaction diagram
-
-
-
-
?
starch + H2O
maltose
show the reaction diagram
-
-
-
-
?
starch + H2O
maltose
show the reaction diagram
-
-
-
-
?
starch + H2O
maltose
show the reaction diagram
-
-
-
?
starch + H2O
maltose
show the reaction diagram
-
-
-
?
starch + H2O
maltose
show the reaction diagram
Sorghum sp.
-
-
-
-
?
starch + H2O
maltose
show the reaction diagram
-
-
-
-
?
starch + H2O
maltose
show the reaction diagram
O23553
-
-
-
?
starch + H2O
maltose
show the reaction diagram
Q9LIR6
-
-
-
?
starch + H2O
maltose
show the reaction diagram
-
-
-
-
?
starch + H2O
maltose
show the reaction diagram
D0VBH4, -
-
-
-
?
starch + H2O
maltose
show the reaction diagram
-
-
beta-maltose
?
starch + H2O
maltose
show the reaction diagram
-
soluble
-
-
?
starch + H2O
maltose
show the reaction diagram
-
soluble
-
?
starch + H2O
maltose
show the reaction diagram
-
soluble
-
-
?
starch + H2O
maltose
show the reaction diagram
-
soluble
-
?
starch + H2O
maltose
show the reaction diagram
-
soluble
-
?
starch + H2O
maltose
show the reaction diagram
-
soluble
-
-
?
starch + H2O
maltose
show the reaction diagram
-
soluble
-
-
?
starch + H2O
maltose
show the reaction diagram
-
soluble
-
-
?
starch + H2O
maltose
show the reaction diagram
-
soluble
-
-
?
starch + H2O
maltose
show the reaction diagram
-
soluble
-
-
?
starch + H2O
maltose
show the reaction diagram
-
soluble
-
-
?
starch + H2O
maltose
show the reaction diagram
-
soluble
-
?
starch + H2O
maltose
show the reaction diagram
-
soluble
-
-
?
starch + H2O
maltose
show the reaction diagram
-
soluble
-
-
?
starch + H2O
maltose
show the reaction diagram
-
soluble
beta-maltose
?
starch + H2O
maltose
show the reaction diagram
-
soluble
beta-maltose
?
starch + H2O
maltose
show the reaction diagram
-
soluble
beta-maltose
?
starch + H2O
maltose
show the reaction diagram
Dioscorea batatus
-
soluble
beta-maltose
?
starch + H2O
maltose
show the reaction diagram
-
soluble starch
-
-
?
starch + H2O
maltose
show the reaction diagram
O23553, Q9LIR6
soluble starch
-
-
?
starch + H2O
maltose
show the reaction diagram
-
raw starch from corn and potato, degradation of starch granules by the enzyme alone occurs at the equatorial grooves of lecticular granules
-
-
?
starch + H2O
maltose
show the reaction diagram
-
potato starch
-
?
starch + H2O
maltose
show the reaction diagram
-
potato starch
-
?
starch + H2O
maltose
show the reaction diagram
-
raw starch from wheat, corn, potato and rice
-
-
?
starch + H2O
maltose
show the reaction diagram
-
gelatinized starch
-
-
?
starch + H2O
maltose
show the reaction diagram
-
boiled
-
-
?
starch + H2O
maltose
show the reaction diagram
-
grains
-
-
-
starch + H2O
maltose
show the reaction diagram
O23553
enzyme induction upon a cold shock at 4C leads to starch-dependent maltose accumulation, which might be required for protection of the photosynthetic electron transport chain and sensitization of PSII during freezing, maltose influences the carbohydrate metabolism, overview
-
-
?
starch + H2O
maltose
show the reaction diagram
-
in roots during storage, the starch hydrolysis at low temperatures is required for improvement of gustative quality of roots from tuberous-rooted chervil, at higher storage temperature the alpha-amylase activity is increased
-
-
?
starch + H2O
maltose
show the reaction diagram
-
role of beta-amylase in starch breakdown during temperature stress, product maltose acts as a cryoprotectant and precursor of soluble sugar metabolism, overview
-
-
?
starch + H2O
maltose
show the reaction diagram
O23553, Q9LIR6
the isozyme is involved in leaf starch degradation
-
-
?
starch + H2O
maltose
show the reaction diagram
-
millet starch, gelatinization temperature is 61.1-68.7C
-
-
?
starch + H2O
maltose
show the reaction diagram
-
soluble starch, depolymerization, reaction scheme
-
-
?
starch + H2O
maltose
show the reaction diagram
Sorghum sp.
-
Sorghum starch, gelatinization temperature is 70-75C
-
-
?
starch + H2O
maltose
show the reaction diagram
-
waxy from maize
-
-
?
starch + H2O
maltose
show the reaction diagram
Paenibacillus polymyxa No. 26-1
-
soluble, raw starch from corn and potato, degradation of starch granules by the enzyme alone occurs at the equatorial grooves of lecticular granules
-
-
?
starch + H2O
maltose
show the reaction diagram
Bacillus megaterium B6
-
-
-
-
?
starch + H2O
maltose
show the reaction diagram
Paenibacillus polymyxa No. 72
-
-
beta-maltose
?
starch + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
starch + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
starch + H2O
beta-maltose
show the reaction diagram
P10537
-
-
-
?
starch + H2O
beta-maltose
show the reaction diagram
-
best substrate, pure and low quality starches, maize starch, tapioca starch
maltose is the major end product, traces of maltooligosaccharides, no glucose as product
-
?
starch + H2O
beta-maltose
show the reaction diagram
-
beta-amylase is involved in starch degradation during mango ripening, which is clearly triggered by detachment from the mother-plant
-
-
?
starch + H2O
beta-maltose
show the reaction diagram
Bacillus megaterium B6
-
best substrate, pure and low quality starches, maize starch, tapioca starch
maltose is the major end product, traces of maltooligosaccharides, no glucose as product
-
?
starch + H2O
maltose + ?
show the reaction diagram
-
-
-
-
?
starch + H2O
maltose + ?
show the reaction diagram
Q9RM92
-
-
-
?
starch + H2O
maltose + ?
show the reaction diagram
-, Q9FQ07
catalyzes the release of maltose residues, starch and amylopectin are better substrates than amylose
-
-
?
starch + H2O
maltose + ?
show the reaction diagram
Bacillus megaterium DSM319
Q9RM92
-
-
-
?
starch + H2O
beta-maltose + ?
show the reaction diagram
-
-
-
-
?
maltotriose + H2O
?
show the reaction diagram
-
very poor substrate
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
soybean trypsin inhibitor and beta-amylase induce rat alveolar macrophages to release nitrogen oxides
-
-
-
additional information
?
-
-
moderately branched glucans are better substrates than less branched or non-branched or highly branched glucans
-
-
-
additional information
?
-
Dioscorea batatus
-
no activity with cyclodextrins
-
-
-
additional information
?
-
-
no hydrolysis of beta-limit dextrin
-
-
-
additional information
?
-
-
no hydrolysis of beta-limit dextrin
-
-
-
additional information
?
-
-
no hydrolysis of beta-limit dextrin
-
-
-
additional information
?
-
-
no activity with maltotriose and cycloheptaose
-
-
-
additional information
?
-
-
no activity with pullulan
-
-
-
additional information
?
-
-
no activity with pullulan
-
-
-
additional information
?
-
-
no activity with pullulan
-
-
-
additional information
?
-
-
no hydrolysis of alpha-1,6-glucosidic linkages
-
-
-
additional information
?
-
-
germination markedly increases the beta-amylase
-
-
-
additional information
?
-
-, Q9FQ07
rhizome beta-amylase is a cytoplasmic vegetative storage protein
-
-
-
additional information
?
-
P36924
beta-amylase does not catalyze a transglycosylation reaction
-
-
-
additional information
?
-
-, Q9FQ07
beta-amylase exclusively catalyzes the release of beta-maltose from the non-reducing ends of alpha-1,4-linked oligo- and polyglucans, three-dimensional structure
-
-
-
additional information
?
-
-
cysteine, tryptophan and serine are essential amino acids for catalysis, not: maltotriose
-
-
-
additional information
?
-
-
not: xylan, pullulan, cellulose, carboxymethyl cellulose
-
-
-
additional information
?
-
-
plants mechanism of cold adaptation, enzyme regulation by phytohormones, light, and by abiotic stess, e.g. by osmotic, cold, salt, and drought stress, the enzyme is also regulated by the circadian clock, detailed overview
-
-
-
additional information
?
-
O23553, Q9LIR6
the isozyme TR-BAMY is redox- and thioredoxin-regulated involving residues C470 and C32 forming a disulfide bridge, the precursor enzyme conatining the transit pepetide is inactive
-
-
-
additional information
?
-
-
starch gelatinization assay, overview
-
-
-
additional information
?
-
-
beta-amylase is an exo-enzyme that specifically binds to a double (1-4-alpha-D-glucopyranosyl-1-4-alpha-D-glucopyranosyl-) unit from the non-reducing ends of polymaltosidic polysaccharides, and sequentially cleaves glucose disaccharidic units until it encounters any structural variation, producing maltose as sole hydrolysis product
-
-
-
additional information
?
-
-
maltose is the main product of soluble starch hydrolysis
-
-
-
additional information
?
-
-, Q8U2G5
the enzyme does not hydrolyze starch, glycogen, pullulan or large maltooligosaccharides
-
-
-
additional information
?
-
Xanthophyllomyces dendrorhous CECT1690
-
cysteine, tryptophan and serine are essential amino acids for catalysis, not: maltotriose
-
-
-
additional information
?
-
Bacillus megaterium B6
-
not: xylan, pullulan, cellulose, carboxymethyl cellulose
-
-
-
additional information
?
-
-
maltose is the main product of soluble starch hydrolysis
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
amylopectin + H2O
maltose
show the reaction diagram
-
-
-
-
?
amylopectin + H2O
maltose
show the reaction diagram
P36924
-
-
-
?
amylopectin + H2O
maltose
show the reaction diagram
Sorghum sp.
-
from starch, preferred substrate
-
-
?
amylopectin + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
amylose + H2O
maltose
show the reaction diagram
Sorghum sp.
-
from starch
-
-
?
starch + H2O
?
show the reaction diagram
-
beta-amylase should be a key enzyme in starch degradation during the germination of millet seeds, enzyme activity increases during days 1-4 of germination
-
-
?
starch + H2O
maltose
show the reaction diagram
-
-
-
-
?
starch + H2O
maltose
show the reaction diagram
-
-
-
-
?
starch + H2O
maltose
show the reaction diagram
-
-
-
-
?
starch + H2O
maltose
show the reaction diagram
Sorghum sp.
-
-
-
-
?
starch + H2O
maltose
show the reaction diagram
O23553, Q9LIR6
-
-
-
?
starch + H2O
maltose
show the reaction diagram
-
-
-
-
?
starch + H2O
maltose
show the reaction diagram
D0VBH4, -
-
-
-
?
starch + H2O
maltose
show the reaction diagram
O23553
enzyme induction upon a cold shock at 4C leads to starch-dependent maltose accumulation, which might be required for protection of the photosynthetic electron transport chain and sensitization of PSII during freezing, maltose influences the carbohydrate metabolism, overview
-
-
?
starch + H2O
maltose
show the reaction diagram
-
in roots during storage, the starch hydrolysis at low temperatures is required for improvement of gustative quality of roots from tuberous-rooted chervil, at higher storage temperature the alpha-amylase activity is increased
-
-
?
starch + H2O
maltose
show the reaction diagram
-
role of beta-amylase in starch breakdown during temperature stress, product maltose acts as a cryoprotectant and precursor of soluble sugar metabolism, overview
-
-
?
starch + H2O
maltose
show the reaction diagram
O23553, Q9LIR6
the isozyme is involved in leaf starch degradation
-
-
?
starch + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
starch + H2O
beta-maltose
show the reaction diagram
-
-
-
-
?
starch + H2O
beta-maltose
show the reaction diagram
P10537
-
-
-
?
starch + H2O
beta-maltose
show the reaction diagram
-
beta-amylase is involved in starch degradation during mango ripening, which is clearly triggered by detachment from the mother-plant
-
-
?
starch + H2O
?
show the reaction diagram
Syncephalastrum racemosum RR96
-
-
-
-
?
maltotetraose + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
germination markedly increases the beta-amylase
-
-
-
additional information
?
-
-, Q9FQ07
rhizome beta-amylase is a cytoplasmic vegetative storage protein
-
-
-
additional information
?
-
-
plants mechanism of cold adaptation, enzyme regulation by phytohormones, light, and by abiotic stess, e.g. by osmotic, cold, salt, and drought stress, the enzyme is also regulated by the circadian clock, detailed overview
-
-
-
additional information
?
-
O23553, Q9LIR6
the isozyme TR-BAMY is redox- and thioredoxin-regulated involving residues C470 and C32 forming a disulfide bridge, the precursor enzyme conatining the transit pepetide is inactive
-
-
-
additional information
?
-
-
maltose is the main product of soluble starch hydrolysis
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2-mercaptoethanol
-
activates
BaCl2
-
1 mM, activates
Ca2+
-
100 mM CaCl2, 29% stimulation
Ca2+
-
one Ca2+ is bound per molecule of enzyme far from the active site
Ca2+
-
activates
CaCl2
-
1 mM, activates
CoCl2
-
1 mM, activates
cysteine
-
activates
dithiothreitol
-
activates
K+
-
100 mM, 20-30% stimulation
NaCl
-
100 mM, 28% stimulation
NaCl
-
activates, best at 10-12% activity drops off dramatically at low NaCl concentrations
SrCl2
-
1 mM, activates
MnCl2
-
1 mM, activates
additional information
-
no requirement for metal ions
additional information
-, Q8U2G5
the presence or absence of various divalent cations or EDTA had a minimal effect on enzyme activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,3-epoxypropyl-alpha-D-glucopyranoside
-
affinity-labeling reagent, mode of binding, covalently bound to the catalytic residue Glu-172, inactivation mechanism
3,4-epoxybutyl-alpha-D-glucopyranoside
-
affinity-labeling reagent, mode of binding, covalently bound to the catalytic residue Glu-172
4-chloromercuribenzoate
-
inactivation, the enzyme can be reactivated by L-cysteine
5,5'-dithiobis-(2-nitrobenzoic acid)
-
chemical modificationof the exposed sulfhydryl groups in beta-amylase from unmalted seeds with 5,5'-dithiobis-(2-nitrobenzoic acid) results in loss of activity. In the beta-amylase from malted seed the 5,5'-dithiobis-(2-nitrobenzoic acid) chemical modification results in the increase in the KM from 2.81 to 4.14 mg/ml
5,5'-dithiobis-2-nitrobenzoate
-
weak
Ag+
-
0.001-0.1 mM AgNO3
Ag+
-
1 mM, almost complete inhibition of mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
Ag+
-
1 mM, almost complete inhibition of recombinant enzyme
AgNO3
-
1 mM, 94% inhibition
Al2(SO4)3
-
1 mM, 57% inhibition
alpha-cyclodextrin
-
-
alpha-cyclodextrin
-
-
alpha-cyclohexaamylose
-
-
beta-amylase-inhibitor
-
several strains of Streptomyces produce a beta-amylase inhibitor when grown on a medium containing starch and deoxynojirimycin
-
beta-cyclodextrin
-
-
Bi(NO3)3
-
1 mM, 54% inhibition
Ca2+
-
binds at the active site
Cd2+
-
1 mM, almost complete inhibition of barley enzyme and recombinant enzyme, less inhibitory towards mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
Cd2+
-
1 mM, almost complete inhibition of recombinant enzyme
Cu2+
-
1 mM CuSO4, 50% inhibition
Cu2+
-
1 mM, almost complete inhibition of mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
Cu2+
-
1 mM, almost complete inhibition of recombinant enzyme
Cu2+
-
5 mM, 37C, 30 min, about 80% inhibition
CuCl2
-
1 mM, 93% inhibition
cyclohexaamylose
-, Q9FQ07
iodine staining method, competitive inhibition
cyclohexaamylose
-
alpha-CD, competitive inhibitor
D-glucose
-, Q9FQ07
p-nitrophenylmaltopentaoside hydrolysis: 125 mM, 87.5% inhibition, iodine staining method: mixed-type, weak inhibition compared with maltose and cyclohexaamylose
D-glucose
-
mode of binding in the active site cleft
D-maltose
-, Q9FQ07
-
D-maltose
-
mode of binding in the active site cleft
D-mannose
-, Q9FQ07
125 mM, 6% inhibition, p-nitrophenylmaltopentaoside hydrolysis
diethyl dicarbonate
-
complete inhibition
EDTA
-
non-competitive, Ca2+ fully restores activity
Fe2+
-
-
-
FeCl3
-
1 mM, 16% inhibition
Hg2+
-
0.001-0.1 mM HgCl2
Hg2+
-
1 mM, almost complete inhibition of mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
Hg2+
-
1 mM, almost complete inhibition of recombinant enzyme
Hg2+
-
5 mM, 37C, 30 min, about 80% inhibition
HgCl2
-
1 mM, 93% inhibition
HgCl2
-
10 mM, 100% inhibition
iodoacetamide
-
-
iodoacetamide
-
-
iodoacetamide
-
-
iodoacetic acid
-
partial
Iodosobenzoate
-
-
maltitol
-
behaves as a mixed-type or competitive inhibitor depending on the chain length of the substrate, inhibition mechanism, binds to Site2 in domain B and forms an abortive ESI complex when amylose is used as substrate
maltose
-
competitive
maltose
-
inhibits light amylase
maltose
-, Q9FQ07
p-nitrophenylmaltopentaoside hydrolysis: 125 mM, 87.5% inhibition, iodine staining method: competitive inhibition
Mg2+
-
binds at the active site
N-bromosuccinimide
-
0.4 mM
N-bromosuccinimide
-
1 mM, 84% inhibition
N-ethylmaleimide
-
remarkably reduces activity
N-ethylmaleimide
-
10 mM, 73% inhibition
N-ethylmalimide
-
-
NaNO2
-
partial
O-alpha-D-glucopyranosyl(1-4)O-alpha-D-glucopyranosyl(1-4)D-xylopyranose
-
mode of binding in the active site cleft
O-alpha-D-xylopyranosyl(1-4)O-alpha-D-glucopyranosyl(1-4)O-alpha-D-glucopyranoside
-
mixed-type inhibition, two molecules bind to enzyme
p-chloromercuribenzoate
-
1 mM, 97% inhibition, exogenous thiols like dithiothreitol, 2-mercaptoethanol or cysteine HCl reactivate
p-chloromercuribenzoate
-
0.01 mM, 100% inhibition
p-Chloromercuriphenyl sulfonic acid
-
-
p-hydroxymercuribenzoate
-
0.5 mM, 96% inhibition
p-methylsulfonylfluoride
-
3 mM, 100% inhibition
PCMB
-
cysteine reactivates
PCMB
-
0.001-0.1 mM, inactivation is partly reversed by adding 10fold to 20fold excess of glutathione or 1,2-dithiopropanol
PCMB
-
0.5 mM, 75% loss of activity after 30 min at 22C, cysteine reactivates
PCMB
-
cysteine reactivates
PCMB
-
restored by mercaptoethanol or dithiothreitol
PCMB
-
0.1 mM, complete inhibition of mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
PCMB
-
0.1 mM, complete inhibition of recombinant enzyme
Phenylarsine oxide
-
complete inhibition
Phenylglyoxal
-
3 mM, 27% inhibition
potassium ferricyanide
-
oxidation of the sulfhydryl groups of the enzyme from malted seed in presence of urea results in formation of a dimeric enzyme. The oxidative dimerization leads to inactivation of the enzyme
Schardinger maltodextrins
-
partial
-
Sodium deoxycholate
-
0.001%, 15% inhibition
Sodium dodecyl sulfate
-
0.001%, 57% inhibition
starch
-
at high concentration s
Trypsin inhibitor
-
-
-
Tween 20
-
0.001%, 16% inhibition
Tween 40
-
0.001%, 15% inhibition
Zn2+
-
1 mM, almost complete inhibition of barley enzyme and recombinant enzyme, less inhibitory towards mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
Zn2+
-
1 mM, almost complete inhibition of recombinant enzyme
Zn2+
-
binds at the active site
ZnSO4
-
1 mM, 54% inhibition
Mn2+
-
5 mM, 37C, 30 min, about 80% inhibition
additional information
-, Q9FQ07
not inhibited by 250 mM lactose
-
additional information
-
the synthesis of beta-amylase is repressed by glucose, fructose or sucrose as carbon source, not inhibited by EDTA
-
additional information
-
no inhibition by 4-chloromercuribenzoate, heavy metal ions, nor Schardinger dextrins
-
additional information
O23553, Q9LIR6
the 41 amino acid transit peptide inhibits isozyme TR-BAMY
-
additional information
-
PMSF and 2-mercaptoethanol have no significant effect on the amylase activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
1 mM, activates
polyethylene glycol 1000
-
1500 Da PEG, increases the enzyme activity by 60% at 0.02% w/v
polyethylene glycol 1500
-
1500 Da PEG, increases the enzyme activity by 77% at 0.02% w/v
-
polyethylene glycol 2000
-
1500 Da PEG, increases the enzyme activity by 58% at 0.02% w/v
polyethylene glycol 400
-
1500 Da PEG, increases the enzyme activity by 7% at 0.02% w/v
-
polyethylene glycol 4600
-
1500 Da PEG, increases the enzyme activity by 74% at 0.02% w/v
polyethylene glycol 600
-
1500 Da PEG, increases the enzyme activity by 19% at 0.02% w/v
polyethylene glycol 8000
-
1500 Da PEG, increases the enzyme activity by 68% at 0.02% w/v
Polyvinyl alcohol
-
10 kDa: increases the enzyme activity by 36% at 0.02% w/v, 50 kDa: increases the enzyme activity by 21% at 0.02% w/v
reduced DTT
O23553, Q9LIR6
strong activation of isozyme TR-BAMY
thioredoxin
O23553, Q9LIR6
thioredocins f1, m1, and y1, the isozyme TR-BAMY is positively thioredoxin-regulated
Triton X-100
-
increases the enzyme activity by 55% at 0.02% w/v
additional information
-
the synthesis of beta-amylase is induced by starch and maltose
-
additional information
-
low temperature of 4C rapidly induces the enzyme activity
-
additional information
-
cold stress activates the chloroplastic isozyme by 5fold at 3C
-
additional information
O23553
the enzyme is induced during low temperature stress at 4C
-
additional information
O23553, Q9LIR6
the enzyme requires reducing conditions for full activity
-
additional information
-
rapid induction of type II beta-amylase by nitric oxide, from sodium nitroprusside, but not by gibberellin in seeds during the early stage of germination, sodium nitroprusside also directly induces the release of the enzyme from glutenin
-
additional information
-
phenylmethanesulfonyl fluoride does not show any effect on enzyme activity
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0827
-
4-nitrophenyl alpha-maltopyranoside
-, Q8U2G5
pH 7.0, 90C
-
0.13
0.17
amylodextrin
-
chain lengths geater than 50
-
0.26
-
Amylopectin
-
pH 5.4, 37C, recombinant mutant T342A
0.39
-
Amylopectin
-
pH 5.4, 37C, recombinant mutant T342S
0.47
-
Amylopectin
P36924
37C, recombinant mutant T47M/Y164E/T328N
0.73
-
Amylopectin
P36924
37C, recombinant wild-type enzyme
0.92
-
Amylopectin
P36924
37C, recombinant mutant Y164F
1.22
-
Amylopectin
P36924
37C, recombinant mutant Y164Q
1.24
-
Amylopectin
P36924
37C, recombinant mutant Y164E
1.84
-
Amylopectin
-
pH 5.4, 37C, recombinant mutant T342V
1.94
-
Amylopectin
-
pH 5.4, 37C, recombinant wild-type enzyme
2.63
-
Amylopectin
P36924
37C, recombinant mutant Y164H
0.491
-
Amylose
-
DP = 17, mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
0.6
-
Amylose
-
pH 7, 25C, DPn: 16, S235A/Y249A/W449F/W495F quadruple mutant
0.61
-
Amylose
-
pH 7, 25C, DPn: 16, W449F/W495F double mutant
0.65
-
Amylose
-
pH 7, 25C, DPn: 16, S235A/Y249A double mutant
0.7
-
Amylose
-
pH 7, 25C, DPn: 16, S235A mutant
0.71
-
Amylose
-
pH 7, 25C, DPn: 16, Y249A mutant
0.72
-
Amylose
-
pH 7, 25C, DPn: 16, wild-type enzyme
94.5
-
maltal
-
-
0.16
-
maltodextrin
-
with 50 glucose equivalents per chain
0.17
-
maltodextrin
-
with 98 glucose equivalents per chain
0.36
-
maltodextrin
-
with 31 glucose equivalents per chain
0.67
-
maltodextrin
-
with 16 glucose equivalents per chain
1.3
-
maltodextrin
-
with 9 glucose equivalents per chain
0.9
-
maltoheptaose
-
-
1.83
-
maltoheptaose
-
mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
0.89
-
maltohexaose
-
-
2
-
maltohexaose
-
mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
1.02
-
maltopentaose
-
-
1.94
-
maltopentaose
-
pH 5.4, 37C, wild-type enzyme
2.02
-
maltopentaose
-
pH 5.4, 37C, mutant E380Q
2.15
-
maltopentaose
-
pH 5.4, 37C, mutant E186Q
2.83
-
maltopentaose
-
mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
0.73
-
p-nitrophenylmaltopentaoside
-
-
0.00317
-
starch
-
pH 5, 40C, soluble starch, V233A mutant of Sd1
0.0033
-
starch
-
pH 5, 40C, soluble starch, wild-type Sd1
0.0036
-
starch
-
pH 5, 40C, soluble starch, R115C mutant of Sd2L
0.00825
-
starch
-
pH 5, 40C, soluble starch, V233A mutant of Sd2L
0.0083
-
starch
-
pH 5, 40C, soluble starch, wild-type Sd2H and V233A/L347S double mutant of Sd2L
0.00831
-
starch
-
pH 5, 40C, soluble starch, wild-type Sd2L
0.00834
-
starch
-
pH 5, 40C, soluble starch, L347S mutant of Sd2L
0.00838
-
starch
-
pH 5, 40C, soluble starch, V430A mutant of Sd2L
0.00856
-
starch
-
pH 5, 40C, soluble starch, D165E mutant of Sd2L
0.77
-
starch
-
soluble
4.17
-
maltotetraose
-
mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
additional information
-
additional information
-
Km: 1.67 mg/ml for soluble starch
-
additional information
-
additional information
-
Km: 2.29 mg/ml for soluble starch at 60C, 1.68 mg/ml for soluble starch at 75C
-
additional information
-
additional information
-
Km: 1.25 mg/ml for starch
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
Km for soluble starch is 0.4%
-
additional information
-
additional information
-
5.9 mg/ml for soluble starch, light amylase. 6.8 mg/ml for soluble starch for soluble starch, heavy amylase
-
additional information
-
additional information
-
Km: 2.25 mg/ml for amylopectin for isoenzyme 2, Km: 1.65 mg/ml for amylopectin, isoenzyme 6
-
additional information
-
additional information
-
Km: 3 mg/ml for soluble starch
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
the Km-value for linear maltodextrins decreases with chain-lengths up to about 50 glucose units and with longer chain lengths it remains constant at about 0.14 mM
-
additional information
-
additional information
-
Km with amylase is 0.24%
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
Km for starch is 4.34 mg/ml at 60C
-
additional information
-
additional information
P16098
beta-amylase from germinated barley has a higher substrate binding affinity for starch than enzyme from mature grain, removal of the four C-terminal glycine-rich repeats enhances the substrate binding affinity, kinetic parameters for several deletion mutants
-
additional information
-
additional information
-
binding parameters of wild-type and mutant enzymes to raw corn starch
-
additional information
-
additional information
-
kinetic parameters for wild-type and mutant SBA
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
the 3 allelic forms of beta-amylase Sd1, Sd2H and Sd2L exhibit different kinetic properties, an R115C mutation is responsible for this difference
-
additional information
-
additional information
P36924
kinetics, recombinant wild-type andmutant enzymes
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
kinetics, isothermal titration microcalorimetric method
-
additional information
-
additional information
-
13.6 mg/l, starch as substrate
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
962
-
4-nitrophenyl alpha-maltopyranoside
-, Q8U2G5
pH 7.0, 90C
-
0.24
-
Amylopectin
-
pH 5.4, 37C, recombinant mutant T342V
0.75
-
Amylopectin
-
pH 5.4, 37C, recombinant mutant T342A
3.5
-
Amylopectin
-
pH 5.4, 37C, recombinant mutant T342S
92
-
Amylopectin
P36924
37C, recombinant mutant Y164H
98.4
-
Amylopectin
-
pH 5.4, 37C, recombinant mutant T342V
325
-
Amylopectin
P36924
37C, recombinant mutant T47M/Y164E/T328N
453
-
Amylopectin
P36924
37C, recombinant mutant Y164Q
550
-
Amylopectin
-
-
988
-
Amylopectin
P36924
37C, recombinant mutant Y164F
1129
-
Amylopectin
P36924
37C, recombinant mutant Y164E
1280
-
Amylopectin
-
pH 5.4, 37C, recombinant wild-type enzyme
2739
-
Amylopectin
P36924
37C, recombinant wild-type enzyme
2400
-
Amylose
-
-
0.034
-
maltopentaose
-
pH 5.4, 37C, mutant E380Q
0.08
-
maltopentaose
-
pH 5.4, 37C, mutant E186Q
299
-
starch
-
pH 5, 40C, soluble starch, wild-type Sd2L
305
-
starch
-
pH 5, 40C, soluble starch, wild-type Sd1
308
-
starch
-
pH 5, 40C, soluble starch, wild-type Sd2H and V233A/L347S double mutant of Sd2L
309
-
starch
-
pH 5, 40C, soluble starch, L347S and R115C mutants of Sd2L
314
-
starch
-
pH 5, 40C, soluble starch, V233A mutant of Sd1
315
-
starch
-
pH 5, 40C, soluble starch, V233A mutant of Sd2L
319
-
starch
-
pH 5, 40C, soluble starch, D165E and V430A mutants of Sd2L
1260
1280
starch
-
pH 5.4-6.0, major isozyme
5460
-
starch
-
from potato
6540
-
starch
-
soluble starch
1280
-
maltopentaose
-
pH 5.4, 37C, wild-type enzyme
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
P16098
kinetic parameters for several deletion mutants
-
additional information
-
additional information
-
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
13.1
13.4
Ca2+
-
pH 4.8, 27C
0.36
-
cyclohexaamylose
-, Q9FQ07
pH 5, 20C, iodine staining method
0.8
-
cyclohexaamylose
-
pH 7, 25C, wild-type enzyme, amylose as substrate
262
-
D-glucose
-, Q9FQ07
pH 5, 20C, iodine staining method
11.7
-
D-maltose
-, Q9FQ07
pH 5, 20C, iodine staining method
2.8
-
maltitol
-
pH 7, 25C, wild-type enzyme, amylose as substrate
3.1
-
maltitol
-
pH 7, 25C, wild-type enzyme, maltopentaose as substrate
5.1
-
maltitol
-
pH 7, 25C, S235A/Y249A double mutant, amylose as substrate
5.7
-
maltitol
-
pH 7, 25C, S235A/Y249A/W449F/W495F quadruple mutant, amylose as substrate
0.45
-
O-alpha-D-xylopyranosyl(1-4)O-alpha-D-glucopyranosyl(1-4)O-alpha-D-glucopyranoside
-
pH 7, 25C, wild-type enzyme, amylose as substrate
17.5
17.7
Zn2+
-
pH 4.8, 27C
18.6
-
Mg2+
-
pH 4.8, 27C
additional information
-
additional information
-
inhibition kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0685
-
-
pH 5.5, 50C
45.95
-
Sorghum sp.
-
96 h germination, the enzyme activity increases progressively during seed germination, overview
100
-
-
-
103.9
-
-
pH 4.5, 37C, soluble starch
161
-
Dioscorea batatus
-
-
300
-
-
-
986
-
P10537
A-7005; type I-B
1030
-
-
-
1077
-
-
-
1187
-
-
-
4464
-
-
variant Tainung No.57
4664
-
-
variant Chailai
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
isoenzyme 6
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
strain 45
additional information
-
-
catalytic activity of the enzyme at different pressure/temperature conditions, up to 700 mPa, 20-70C, overview
additional information
-
-
the enzyme activity increases progressively during seed germination, different cultivars, activity in phoshate buffer extracts, the activity is decreased in hot water extracts, and highly decreased in cold water extracts, overview the hot water extracts show higher activity due to gelatinization of the starch grains
additional information
-
-
-
additional information
-
Sorghum sp.
-
different increase in activities during seed germination in the different Sorghum sp. varieties, overview
additional information
-
O23553
-
additional information
-
Q6Z5B2, Q6Z5B7
very low activity in different cultivars of varieties japonica and japonica x indica, i.e. Nipponbare x Kasalath, the Nipponbare allele highly suppresses the enzyme, quantitative activity and expression analysis; very low activity in different cultivars of varieties japonica and japonica x indica, i.e. Nipponbare x Kasalath, the Nipponbare allele highly suppresses the enzyme, quantitative activity and expression analysis
additional information
-
-
BAM-2 specific activity is 25fold lower than that of BAM-3 and 50fold lower than that of BAM-1. No activity is detectable for recombinant BAM-4 protein
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.5
7.5
-
-
4
5
-
acetate buffer
4.2
-
P36924
mutant Y164Q
4.6
-
P36924
mutant Y164E
4.8
-
-, Q9FQ07
-
4.8
-
P36924
mutants Y164H and Y164F
4.8
-
-
assay at
5
6.5
-
hydrolysis of gelatinized starch
5
-
P16098
assay at, potato starch as substrate
5
-
-
assay at, starch as substrate
5.4
6
-
-
5.4
-
-
isoenzyme 2 and 6
5.4
-
-
hydrolysis of potato amylopectin, at 37C, the reduced pKa-value of Glu-380 is stabilized by the hydrogen bond network and is responsible for the lower pH-optimum of soybean beta-amylase compared with that of Bacillus cereus, pH 6.7
5.4
-
-
-
5.4
-
-
assay at
5.5
6
-
citrate buffer
5.5
6
-
hydrolysis of boiled soluble starch
5.5
6.5
-
-
5.5
7
-
enzyme from strain 45
5.5
-
-
native enzyme
5.5
-
-
degradation of glycogen
5.5
-
-
raw corn starch
6
8
O23553, Q9LIR6
-
6
-
-
immobilized enzyme
6
-
-
-
6
-
Dioscorea batatus
-
-
6
-
P36924
mutant T47M/Y164E/T328N
6
-
-
assay at
6
-
-
assay at, phosphate buffer
6.2
-
P16098
assay at, p-nitrophenylmaltopentaoside as substrate
6.2
-
-
assay at, p-nitrophenylmaltopentaoside as substrate
6.5
-
-
hydrolysis of p-nitrophenylmaltopentaoside
6.5
-
-
enzyme from strain MNU82
6.7
-
P36924
wild-type enzyme
7
-
-
assay at
7
-
-
assay at
7.5
-
Q9RM92
-
7.5
-
-, P06547
assay at
additional information
-
P36924
comparison of pH-dependency/pH-profiles of recombinant wild-type and mutant enzymes
additional information
-
O23553, Q9LIR6
the isozyme TR-BAMY shifts between an active and an inactive form dependent on the pH
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2
8
-
pH 2.0: about 35% of maximal activity, pH 8.0: about 30% of maximal activity
3
7
-, Q9FQ07
active in the range
3
7.2
-
50% of maximal activity at pH 3.0 and pH 7.2, degradation of glycogen
3
7.5
Dioscorea batatus
-
no activity below pH 3.0 and above pH 7.5
3
8
-
pH 3.0: about 35% of maximal activity, pH 8.0: about 70% of maximal activity
3
8
-
pH 3.0: about 70% of maximal activity, pH 8.0: about 60% of maximal activity
3
8
-
pH 3.0: about 50% of maximal activity, pH 8.0: about 55% of maximal activity
3
8.5
-
pH 3.0: about 30% of maximal activity, pH 8.5: about 40% of maximal activity
3
9
-
pH 3.0: about 50% of maximal activity, pH 9.0: about 40% of maximal activity
3
9
-
pH 3.0: about 70% of maximal activity, pH 9.0: about 15% of maximal activity
4
12
-
activity range
4
6.5
-
active in the range
4
7
Dioscorea batatus
-
pH 4.0: about 25% of maximal activity, pH 7.0: about 50% of maximal activity
4
8
-
pH 4.0: about 65% of maximal activity, pH 8.0: about 55% of maximal activity
4.5
8.5
-
pH 4.5: about 40% of maximal activity, pH 8.5: about 60% of maximal activity
5
6
-
more than 80% of maximal activity at pH 5.0 and at pH 6.0
5
8
-
pH 5.0: about 55% of maximal activity, pH 8.0: about 60% of maximal activity
5.5
10
-
pH 5.5.: about 50% of maximal activity, pH 10.0: about 40% of maximal activity
6
9
-
about 75% of maximal activity at pH 6.0 and pH 9.0
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
higher activity of beta-amylase at 4C compared to 10-16 C
20
-
-, Q9FQ07
assay at, starch, amylose or amylopectin as substrate
25
-
-
assay at
25
-
Cenchrus sp., Sorghum sp.
-
assay at
25
-
-
assay at
25
-
P10537
assay at
27
-
-
assay at
37
-
P36924
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
O23553, Q9LIR6
assay at
40
-
-
hydrolysis of p-nitrophenylmaltopentaoside
40
-
P16098
assay at
40
-
-, Q9FQ07
assay at, p-nitrophenylmaltopentaoside as substrate
40
-
-
assay at
40
-
-, P06547
assay at
42
-
-
degradation of glycogen
45
-
-
raw corn starch
50
-
-
native enzyme
50
-
-
gelatinized starch
50
-
Q9RM92
-
55
-
-
immobilized enzyme
55
-
Dioscorea batatus
-
-
55
-
-
original and recombinant enzyme
55
-
-
optimum temperature after 30 min incubation
55
-
-
approximately
60
-
-
-
60
-
-
temperature optimum, but enzyme loses activity when exposed to 60C, irreversible thermodenaturation
65
-
-
mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
70
-
-
native immobilized beta-amylase
75
-
-
hydrolysis of gelatinized starch
75
-
-
chemically modified and subsequently immobilized beta-amylase
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
60
-
active in the range
20
70
-
at different pressure/temperature conditions, up to 700 mPa, overview
28
61
-
28C: about 40% of maximal activity, 61C: about 30% of maximal activity
29
41
-
75% of maximal activity at 29C and at 41C
30
60
-
30C: about 25% of maximal activity, 60C: about 20% of maximal activity, hyrolysis of raw corn starch
40
60
Dioscorea batatus
-
40C: about 30% of maximal activity, 60C: about 50% of maximal activity
45
-
-
beta-amylase hydrolyzes corn starch granules efficiently at 45C, 60% more active than soybean beta-amylase at 45C
45
-
-
at 45C beta-amylase is 60% less active in hydrolysis of corn starch granules than enzyme from Bacillus cereus
50
70
-
50C: about 55% of maximal activity, 70C: about 70% of maximal activity
50
70
-
activity range
50
80
-
50C: about 55% of maximal activity, 80C: about 65% of maximal activity
50
85
-
50C: about 45% of maximal activity, 85C: about 25% of maximal activity
85
90
-
85C: 83% of maximal activity, 90C: 32.8% of maximal activity
additional information
-
O23553
freezing tolerance of recombinant plants, overview
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.45
6.5
-
detailed isoelectric focusing analysis of pI of different isozymes from 17 Hordeum species, some with several suspecies, four pattern groups, overview
4.5
-
-
chromatofocusing
4.6
4.7
-
isoelectric focusing
4.8
6
-
isoelectric focusing analysis of isozyme pI of different cultivars, overview
4.9
-
-, Q9FQ07
isoelectric focusing
4.9
-
-
isoelectric focusing
5.7
-
-
isoenzyme 50KCBA1, isoelectric focusing
5.9
-
-
isoenzyme 50KCBA2, isoelectric focusing
6
-
-
isoenzyme 50KCBA3, isoelectric focusing
6.2
-
-
isoenzyme 50KCBA4, isoelectric focusing
6.4
-
-
isoenzyme 50KCBA5, isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
D0VBH4, -
shoot tip of the bud
Manually annotated by BRENDA team
P16098
mature, of Sd1 and Sd2L barley varieties
Manually annotated by BRENDA team
-
endosperm-specific isozyme beta-amylase1, Bmy1
Manually annotated by BRENDA team
-
BMY is stored in seeds bound to starchy endosperm possibly through S-S bridges, during germination the enzyme is released by proteolytic cleavage resulting in a smaller enzyme form
Manually annotated by BRENDA team
O23553, Q9LIR6
isozyme TR-BAMY
Manually annotated by BRENDA team
Q3S4X4
banana beta-amylase activity is highly correlated to a decrease in starch, being primary up-regulated by de novo synthesis
Manually annotated by BRENDA team
P16098
germinated barley, of Sd1 and Sd2L barley varieties
Manually annotated by BRENDA team
O23553, Q9LIR6
isozyme TR-BAMY
Manually annotated by BRENDA team
O23553, Q9LIR6
isozyme TR-BAMY
Manually annotated by BRENDA team
-, Q9FQ07
resting, localized in the cortex and the pith of rhizomes, but not in vascular tissues, pericycle, endodermis and rhizodermis
Manually annotated by BRENDA team
O23553, Q9LIR6
isozyme TR-BAMY
Manually annotated by BRENDA team
-
endosperm
Manually annotated by BRENDA team
-
germinating
Manually annotated by BRENDA team
Cenchrus sp., Sorghum sp.
-
the enzyme activity increases progressively during seed germination
Manually annotated by BRENDA team
Sorghum sp.
-
germinating, different activities during germination in the different Sorghum sp. varieties, overview
Manually annotated by BRENDA team
-
BMY is stored in seeds bound to starchy endosperm possibly through S-S bridges, during germination the enzyme is released by proteolytic cleavage resulting in a smaller enzyme form
Manually annotated by BRENDA team
-
distribution of thermostable alleles/isozymes in worldwide seed collections, detailed overview
Manually annotated by BRENDA team
O23553, Q9LIR6
isozyme TR-BAMY
Manually annotated by BRENDA team
Q6Z5B2, Q6Z5B7
germinating; germinating
Manually annotated by BRENDA team
-
malted and unmalted
Manually annotated by BRENDA team
-
malted
Manually annotated by BRENDA team
-
epicotyl of etiolated germinating seedlings
Manually annotated by BRENDA team
Q6Z5B2, Q6Z5B7
very low enzyme content in var. japonica; very low enzyme content in var. japonica
Manually annotated by BRENDA team
additional information
-
enzyme is produced throughout exponential growth and during the early-stationary phase
Manually annotated by BRENDA team
additional information
-
differentiation of beta-amylase phenotypes in cultivated barley from worldwide collections, geographical distribution, overview
Manually annotated by BRENDA team
additional information
-
tissue-ubiquitous isozyme beta-amylase2, Bmy2
Manually annotated by BRENDA team
additional information
-
BAM4 is preferentially expressed in vascular tissues in source and sink organs
Manually annotated by BRENDA team
additional information
-
beta-amylase production starts from the post-exponential phase of bacterial growth and reached a maximum level during the early-stationary phase
Manually annotated by BRENDA team
additional information
-
beta-amylase production starts from the post-exponential phase of bacterial growth and reached a maximum level during the early-stationary phase
-
Manually annotated by BRENDA team
additional information
Syncephalastrum racemosum RR96
-
optimal cultivation conditions, overview
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
stroma of mesophyll cell chloroplasts
Manually annotated by BRENDA team
O23553, Q9LIR6
plastid-targeted isozyme CT-BAMY, contains a plastid transit peptide; plastid-targeted isozyme TR-BAMY, contains a plastid transit peptide of 41 amino acids
Manually annotated by BRENDA team
-
BAM-1, BAM-2, BAM-3, BAM-4
Manually annotated by BRENDA team
-, Q9FQ07
exclusively located in
Manually annotated by BRENDA team
D0VBH4, -
BAM1 also surrounds the amyloplasts in mature cells
Manually annotated by BRENDA team
-
biosynthesis of the enzyme is induced by starch or maltodextrin. Glucose is the most potent repressor. The repression is not overcome after the fall of glucose concentration in the culture medium below a critical level. This catabolite repression exerted by glucose is partially relieved by exogenous cGMP and its dibutyryl derivative. GMP restores the original extent of enzyme synthesis in glucose repressed cells
-
Manually annotated by BRENDA team
-
the enzyme is secreted
-
Manually annotated by BRENDA team
Bacillus megaterium B6
-
; biosynthesis of the enzyme is induced by starch or maltodextrin. Glucose is the most potent repressor. The repression is not overcome after the fall of glucose concentration in the culture medium below a critical level. This catabolite repression exerted by glucose is partially relieved by exogenous cGMP and its dibutyryl derivative. GMP restores the original extent of enzyme synthesis in glucose repressed cells
-
-
Manually annotated by BRENDA team
Bacillus megaterium DSM319, Emericella nidulans 45
-
-
-
-
Manually annotated by BRENDA team
-
the enzyme is secreted
-
-
Manually annotated by BRENDA team
Paenibacillus polymyxa No. 26-1, Xanthophyllomyces dendrorhous CECT1690
-
-
-
-
Manually annotated by BRENDA team
-
cultivated, thermostable alleles/isozymes of the enzyme
Manually annotated by BRENDA team
O23553, Q9LIR6
plastid-targeted isozyme TR-BAMY, contains a plastid transit peptide of 41 amino acids
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
29000
-
D0VBH4, -
mature BAM1, SDS-PAGE
35000
-
-
gel filtration
35000
-
D0VBH4, -
unprocessed BAM1, SDS-PAGE
41700
-
-
light amylase, gel filtration
44000
-
-
beta-amylase I and II, gel filtration
45000
-
-
gel filtration
53000
-
-
gel filtration, disc gel electrophoresis
54600
-
-
BAM-2
55000
-
-
gel filtration
55000
-
-
amino acid analysis
55500
-
-
BAM-3; calculated, BAM-2
55800
-
-
calculated, BAM-3
55990
-
-
isoenzyme I and II, electrospray ionization mass spectroscopy
56000
-
-
gel filtration
56100
-
-
amino acid analysis
56310
-
-
isoenzyme IV, electrospray ionization mass spectroscopy
57000
-
-
gel filtration
57000
-
-
equilibrium sedimentaion
57200
-
-
equilibrium sedimentation
58000
-
-
gel filtration
58000
-
-
gel filtration
59500
-
-
calculated, BAM-1
60000
-
O23553, Q9LIR6
recombinant mature isozyme TR-BAMY, gel filtration
61000
-
-
DEAE-Sepharose and Sephadex G-100
62000
-
-
gel filtration
62500
-
-
equilibrium sedimentation
64000
-
O23553, Q9LIR6
recombinant precursor isozyme TR-BAMY, gel filtration
65700
-
-
heavy amylase, gel filtration
67500
-
-
BAM-1
105000
-
-
gel filtration
110000
-
-
gel filtration, sucrose density gradient centrifugation, ultracentrifugation
111000
-
-
gel filtration
152000
-
-
calculation from sedimentation and diffusion data
152000
-
-
-
200000
-
-, Q9FQ07
gel filtration
206000
-
-
determination from crystallographic data
209000
-
-
variant Tainung, gel filtration
239000
-
-
variant Chailai, gel filtration
240000
-
-
gel filtration
315000
-
-
enzyme modified with periodate-oxidized maltohexaose, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 61000, SDS-PAGE
?
-
x * 55000, SDS-PAGE
?
-
x * 57000, SDS-PAGE
?
-
x * 53000, SDS-PAGE
?
-
x * 19600, calculation of the minimum molecular weight from amino acid content
?
-
x * 57000, SDS-PAGE
?
Dioscorea batatus
-
x * 60000, SDS-PAGE
?
-
x * 56000, mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S, SDS-PAGE; x * 59144, mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S, calculation from amino acid sequence
?
-
x * 58000, SDS-PAGE
?
-
x * 56000, recombinant enzyme, SDS-PAGE; x * 59169, recombinant enzyme, calculation from amino acid sequence
?
-
x * 58300, Western blot analysis
dimer
-
2 * 56000, SDS-PAGE
homotetramer
-, Q9FQ07
4 * 55000, SDS-PAGE, 4 * 56068, mass spectrometry, 4 * 56204, sequence calculation inclusive the N-terminal methionine
monomer
-
1 * 57000, SDS-PAGE
monomer
-
1 * 60000, SDS-PAGE
monomer
-
1 * 58000, SDS-PAGE
monomer
-
1 * 58000, SDS-PAGE
monomer
-
1 * 45000, SDS-PAGE
monomer
-
1 * 53000, SDS-PAGE
monomer
-
1 * 102000, SDS-PAGE
monomer
-
1 * 58000, SDS-PAGE
monomer
O23553, Q9LIR6
1 * 60000, recombinant mature isozyme TR-BAMY, SDS-PAGE, 1 * 64000, recombinant precursor isozyme TR-BAMY, SDS-PAGE
monomer
-
1 * 56000, SDS-PAGE
monomer
Bacillus megaterium B6
-
1 * 102000, SDS-PAGE
-
pentamer
-
5 * 64000, enzyme modified with periodate-oxidized maltohexaose, SDS-PAGE
tetramer
-
4 * 51000, SDS-PAGE
tetramer
-
4 * 26000, SDS-PAGE
monomer
Paenibacillus polymyxa No. 26-1
-
1 * 53000, SDS-PAGE
-
additional information
-
enzyme is composed of two functional domains, a catalytic domain: domains A and B, and starch-binding domain: domain C, beta-amylase has three carbohydrate-binding sites aside from the active site: two in domain B named Site2 and Site3, one in domain C named Site1, roles of these sites in the catalytic reaction and raw starch-binding
additional information
-
structure analysis, intramolecular hydrogen bond interactions
additional information
-, P06547
three-dimensional structure modelling, overview
additional information
Bacillus circulans NCIMB 11033
-
three-dimensional structure modelling, overview
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
no glycoprotein
-, Q9FQ07
-
glycoprotein
-
0.8% carbohydrate
glycoprotein
Emericella nidulans 45
-
0.8% carbohydrate
-
glycoprotein
-
intracellular enzyme contains 0.8% carbohydrate
no glycoprotein
-
extracellular enzyme contains no carbohydrate moiety
no glycoprotein
-
contains no carbohydrate
no glycoprotein
-
contains no carbohydrate
proteolytic modification
P16098
beta-amylase undergoes proteolytic cleavage of the C-terminal region after germination, removal of the four C-terminal glycine-rich repeats enhances the thermostability and substrate binding affinity
proteolytic modification
-
BMY is stored in seeds bound to starchy endosperm possibly through S-S bridges, during germination the enzyme is released by proteolytic cleavage resulting in a smaller enzyme form, the uncleaved enzyme form shows reduced activity
glycoprotein
-
enzyme form F-A contains 9.7% carbohydrate, enzyme form F-B contains 9.3% carbohydrate
proteolytic modification
-
the 60000 Da enzyme form is 3000 Da larger than the mature enzyme from Bacillus circulans, suggesting that processing of the enzyme is different between the two species
additional information
-, Q9FQ07
apart from the removal of the N-terminal methionine no co- or posttranslational processing
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
beta-amylase complexed with the inhibitors glucose, maltose and O-alpha-D-glucopyranosyl(1-4)O-alpha-D-glucopyranosyl(1-4)D-xylopyranose and the affinity-labeling reagents 2,3-epoxypropyl-alpha-D-glucopyranoside and 3,4-epoxybutyl-alpha-D-glucopyranoside, X-ray analysis
-
crystal structure determined by the multiple isomorphous replacement method
-
purified recombinant wild-type and mutant T47M/Y164E/T328N, hanging drop vapour diffusion method, 18C, 0.005 ml of 15 mg/ml protein in 0.05 M sodium acetate is mixed with 0.005 ml mother liquor containing 15% PEG 6000, 5% saturated ammonium sulfate, 0.1 M phosphate, pH 6.5, crystallization of mutants Y164E and Y164F in the same way except for usage of 0.1 M sodium acetate buffer, pH 4.6, instead of phosphate buffer, X-ray diffraction structure determination and analysis at 1.72-1.95 A resolution, active site structure modelling
P36924
X-ray crystal structures of wild-type enzyme complexed with maltose and of E172A catalytic site mutant complexed with maltopentaose
-
crystal structure of mutant enzyme W55R
-
high-resolution crystal structure for catalytic active enzyme and for the enzyme complexes with either beta-maltose or maltal
-
purified recombinant mutant enzymes, mutant enzyme E186Q in complex with substrate maltopentaose, and mutant enzyme E380Q in complex with product maltose, hanging drop vapour diffusion method, 20 mg/ml protein in 45-50% w/v ammonium sulfate, 0.1 M sodium acetate, pH 5.4, 1 mM EDTA, and 18 mM 2-methyl-2,4-pentanediol, equilibration against 1 ml mother liquor, 4C, soaking of crystals in 30 mM ligand solution, cryoprotection of crystals with 30% v/v glycerol in crystallization solution, X-ray diffraction structure determination and analysis at 1.6 and 1.9 A resolution, respectively, active site structure modelling
-
purified recombinant T342 mutant enzymes, hanging drop vapour diffusion method, 0.005 ml of 10 mg/ml protein solution is mixed with 0.005 ml of reservoir solution containing 40-50% w/v ammonium sulfate, 1 mM EDTA, 18 mM 2-methyl-2,4-pentanediol, and 0.1 M sodium acetate, pH 5.4, equilibration against 1 ml of reservoir solution, 4C, gradual soaking of crystals in 0.1 M sodium acetate, pH 6.1, 50% w/v ammonium sulfate, 1 mM EDTA, 20 mM DTT, 0.3 M maltose, and 30% v/v glycerol, X-ray diffraction structure determination and analysis at 1.12-1.6 A resolution, active site structure modelling
-
wild-type, M51T, E178Y and N340T mutant SBA, complexed with maltose, hanging-drop vapor diffusion method, X-ray analysis
-
mutant M185L/S295A/I297V/S350P/S351P/Q352D/A376S
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2.5
-
-
tertiary structure is entirely disturbed
3
11
-, Q9FQ07
stable in the range
3
12
-, Q9FQ07
irreversible inactivation below pH 3 and above pH 12
3.5
7
-
70C, in presence of 5 mM CaCl2
3.5
9
-
15 h, 20C, 50 mM McIlvaines buffer and sodium carbonate-boric acid buffer, stable in the range
3.5
9.5
-
stable
3.7
-
-
stable
4
12
-
4C, 24 h, stable
4
8
-
50C, 1 h, enzyme retains more than 80% of the activity
4
9
-
15 h, 37C, stable
4.3
8.5
Dioscorea batatus
-
30C, 60 min, stable
4.5
7.5
-
30C, 1.5 h, stable
5
6
-
immobilized enzyme, highest stability
5
-
-
2 months, about 80% loss of activity
6
8
-
37C, 90 min, stable
6
8
-
30 min, stable
6.5
7.5
-
50C, 1 h, stable
6.5
7.5
-
90% stability between pH 6.5 and 7.5
7
11.5
-
20C, 24 h, stable. Sharp decrease in activity at pH 12.0
7.5
-
-
30 min: 50% loss of activity, 60 min: 75% loss of activity, 120 min: 100% loss of activity
9.5
-
-
unstable above, original recombinant enzyme
9.5
-
-
2 months, 60% loss of activity
12.5
-
-
mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S is stable up to
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40
-
-
thermal denaturation above
40
-
-
unstable above
40
-
-
completely stable up to
45
-
-
pH 7.5, 30 min, stable
50
-
-
10 min, stable below
50
-
-
5 h, 45% loss of activity
50
-
-
1 h, stable
50
-
-
10 min, stable below
50
-
-
pH 6.0, 30 min, native enzyme is stable up to
52.6
-
P16098
T50, Sd2L, mature grain
53
-
-
stable up to
54.7
-
P16098
T50, Sd1, mature grain
55
-
-
1 h, 20% loss of activity
55
-
-
pH 6.0, 30 min, immobilized enzyme is stable up to
55
-
-
15 min, 50% loss of activity
55
-
-
2 h, in presence of substrate, stable
55
-
-
30 min, 56% loss of activity
55
-
-
15 min, 50 mM NaOAc buffer, pH 6, stable up to
55.2
-
-
T50 value for wild-type Sd2L and its D165E mutant
55.3
-
-
T50 value for R115C and V430A mutants of Sd2L
57
-
-
30 min, 50% loss of activity; 30 min, recombinant enzyme, 50% loss of activity
57.1
-
-
T50 value for V233A mutant of Sd2L
57.3
-
-
T50 value for wild-type Sd1 and L347S mutant of Sd2L
57.5
-
-
30 min, analysis of isozyme thermostability of different species and subspecies, overview
57.5
-
-
30 min, analysis of isozyme thermostability of different cultivars, overview
59.2
-
-
T50 value for wild-type Sd2H and V233A/L347S double mutant of Sd2L
59.4
-
-
T50 value for V233A mutant of Sd1
60
-
-
more than 2 h, 96% loss of activity
60
-
-
40 min, stable
60
-
-
pH 5.4, 90 min, 38% loss of activity of isoenzyme 2, 55% loss of activity of isoenzyme 6
60
-
-
10 min, about 70% loss of activity
60
-
-
pH 4.8, half-life: 291 min for the first decay segment, 1790 min for the second decay segment
60
-
-
rather stable at
60
-
-
in presence of 5% starch, entirely stable
60
-
-
temperature optimum, but enzyme loses activity when exposed to 60C, irreversible thermodenaturation, thermodenaturation kinetics, Mn2+ and exogenous thiols like dithiothreitol, 2-mercaptoethanol or cysteine HCl play a remarkable role in reactivation of thermally denatured enzyme
60
-
-, Q9FQ07
stable up to
60
-
-
30 min: 65% loss of activity, 60 min: 75% loss of activity, 90 min: 100% loss of activity
60
-
-
the thermoinactivated enzyme (exposed to 60C for 10 min) could be partially reactivated by the addition of 1 mM 2-mercaptoethanol (7.3% increase) and 4 mM Mn2+ (14% increase)
60
-
-, P06547
half-life of the wild-type enzyme is 6.4 min
63
-
-
30 min, 50% loss of activity
65
-
-
1.5 h, retains about 80% of its activity
69
-
-
30 min, mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S, 50% inactivation
70
-
-
2 h, stable in absence of substrate or Ca2+
70
-
-
pH 4.8, half-life: 14.4 min for the first decay segment, 37.9 min for the second decay segment
70
-
-
15 min, stable
70
-
-, Q9FQ07
10 min, complete inactivation
75
-
-
about 20% loss of activity
80
-
-
unstable in absence of substrate or Ca2+, stable in presence of 5 mM Ca2+ or 1% substrate
80
-
-
pH 6.0, 10 min, about 50% loss of activity
additional information
-
-
stability is greatly enhanced by addition of 5 mM CaCl2
additional information
-
-
starch greatly enhances heat stability
additional information
-
-
immobilization of both native and modified enzymes on a amino silica results in thermostabilization of the enzyme
additional information
-
-
the 3 allelic forms of beta-amylase Sd1, Sd2H and Sd2L exhibit different thermostability, due to two amino acid substitutions, V233A and L347S, which increase the thermostability index T50 of Sd2L by 1.9C and 2.1C, respectively
additional information
-
-
thermal inactivation kinetics of the enzyme at different pressure/temperature conditions, mechanism, overview
additional information
-
-
the recombinant isozyme Bmy2 from cultivar Morex shows a slightly higher thermostability compared to the recombinant enzyme from cultivar Steptoe, T50 values, residues D238, M337, and Q362 are involved in the Morex Bmy2 thermostability, overview
additional information
-
-
increased thermoresistance of beta-amylase is achieved through stabilization of thiol groups present at the active site by manipulating the enzymes environment by the addition of Mn2+ and 2-mercaptoethanol, and through immobilization. Both of which would increase the enzymes practical importance and industrial utility
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
immobilization of beta-amylase through gel-entrapment and covalent crosslinking brings about a remarkable increase in thermotolerance with about a 14-fold increase in catalytic half-life
-
guanidine hydrochloride, 6 M, complete disorganization of the secondary structure
-
SDS, effective in disturbing the tertiary structure, no effect on secondary structure
-
enzyme immobilized on p-aminobenzyl-cellulose by diazotization is stable in the dry state for more than 6 months
-
immobilization of both native and modified enzymes on a amino silica results in thermostabilization of the enzyme
-
repeated freezing and thawing results in a large loss of activity
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ethanol
-
10% v/v, 1 h, 65C, completely stable
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
enzyme is oxidatively dimerized by treatemnt with 0.3 M ferricyanide in 3 M urea. The dimerized enzyme is thought to be one of inert beta-amylases in ungerminated seeds
-
208622
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the activity in roots at 4-16C during storage is immediately increased after beginning
-
4C, stable for 3 weeks
-
3C, in presence of 0.05 M beta-mercaptoethanol, 50% loss of activity after 1 week
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
affinity chromatography, to near homogeneity using Glutathione-Sepharose 4B
-
native isozyme partially by chloroplast purification; native isozyme partially by chloroplast purification, recombinant mature isozyme TR-BAMY and recombinant mutant enzymes from Escherichia coli
O23553, Q9LIR6
E172A, E367A and E172A/E367A mutant enzymes
-
recombinant wild-type and mutant enzymes
-
recombinant wild-type and mutant enzymes from Escherichia coli strain XL1-Blue
P36924
gel filtration
-
-
Dioscorea batatus
-
4 isoforms
-
isoenzyme 6
-
mutant beta-amylases
-
recombinant wild-type and mutant enzymes from Escherichia coli strain JM105
-
recombinant wild-type and mutants from Escherichia coli
-
native beta-amylase from both mature grain and germinated barley of Sd1 and Sd2L barley varieties, recombinant beta-amylase
P16098
recombinant enzyme
-
recombinant mutant enzymes
-
multiple forms
-
beta-amylase I and II
-
partially by preparation of enzyme extract and heat treatment at 70C for 20 min
-
partial, 14.67fold
-
continuous extraction in a PEG/CaCl2 aqueous two-phase system. The best system for recovering the maize malt enzymes is with low vane rotation and flux rate and high free area of vane
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
DNA sequence determination, construction of BMY8 knockout plants, and of BMY8 RNAi plants
O23553
expressed in Escherichia coli
-
expression in Escherichia coli as a GST fusion protein; expression in Escherichia coli as a GST fusion protein
O23553, Q9LIR6
isozyme CT-BAMY, DNA and amino acid sequence determination and analysis; isozyme TR-BAMY, DNA and amino acid sequence determination and analysis, functional expression of mature isozyme TR-BAMY and of mutant enzymes in Escherichia coli strains HB101 and BL21(DE3), transient expression of GFP-tagged isozyme TR-BAMY in Nicotiana tabacum protoplasts with exclusive association to the chloroplasts
O23553, Q9LIR6
expression of wild-type and mutant enzymes in Escherichia coli strain XL1-Blue
P36924
wild-type and mutant enzymes, expression in Escherichia coli BL21(DE3)
-
2 active enzyme forms are detected after expression in Escherichia coli, MW 60000 Da and MW 49000 Da. The 60000 Da enzyme form is 3000 Da larger than the mature enzyme from Bacillus circulans, suggesting that processing of the enzyme is different between the two species
-
phylogenetic analysis, expression of wild-type and mutant enzymes in Escherichia coli Rosetta2 cells, subcloning in strain JM109
-, P06547
the bamM gene from Bacillus megaterium DSM319 encoding an extracellular beta-amylase was isolated and completely sequenced
Q9RM92
expression of wild-type and mutant enzymes in Escherichia coli strain JM105
-
expression of wild-type and mutants in Escherichia coli strains JM109 and JM105
-
DNA and amino acid sequence determination and analysis, phylogenetic analysis
-
expression in Escherichia coli, the recombinant enzyme lacks 4 amino acids at positions 2-5 (Glu-Val-Asn-Val) when compared with barley beta-amylase
-
expression of a sevenfold mutant beta-amylase, M185L/S295A/I297V/S350P/S351P/Q352D/A376S
-
isozyme Bmy2 from cultivars Morex and Steptoe, DNA and amino acid sequence determination and analysis, expression in Escherichia coli
-
Sd1 and Sd2L, from developing grain, expression in Escherichia coli M15
P16098
two of the 3 allelic forms of beta-amylase Sd1 and Sd2L are cloned and sequenced
-
expression in Escherichia coli
Q3S4X4
two rice genes encoding the enzyme, genes BAC83770 and BAC83773, in tight linkage, expression analysis, the Nipponbare allele in gene BAC83773 highly suppresses the enzyme; two rice genes encoding the enzyme, genes BAC83770 and BAC83773, in tight linkage, expression analysis, the Nipponbare allele in gene BAC83773 highly suppresses the enzyme
Q6Z5B2, Q6Z5B7
a fusion gene that encodes a polypeptide of 1495 amino acids is constructed from the beta-amylase gene of Clostridium thermosulfurogenes and trehalose synthase gene of Thermus thermophilus. The fused gene is overexpressed in Escherichia coli, and a recombinant bifunctional fusion protein with beta-amylase at the N-terminal or C-terminal of trehalose synthase having both beta-amylase and trehalose synthase activities with an apparent molecular mass of 164000 Da is obtained
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cold-stress treatment, 4C for 24 h
-
the beta-amylase activity is negatively correlated with abscisic acid concentration, exogenous application of H2O2 and ascorbic acid decreases beta-amylase activity in the abscisic acid-sensitive barley mutant TL43
-
the beta-amylase activity is positively correlated with H2O2 concentration, exogenous application of H2O2 and ascorbic acid increases beta-amylase activity in barley variety Triumph
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C148S
O23553, Q9LIR6
site-directed mutagenesis, the mutant shows a redox sensitivity similar to the wild-type enzyme
C206S
O23553, Q9LIR6
site-directed mutagenesis, the mutant shows a redox sensitivity similar to the wild-type enzyme
C261S
O23553, Q9LIR6
site-directed mutagenesis, the mutant shows a redox sensitivity similar to the wild-type enzyme
C32S
O23553, Q9LIR6
site-directed mutagenesis, the mutant shows 70% impaired redox sensitivity compared to the wild-type enzyme
C399S
O23553, Q9LIR6
site-directed mutagenesis, the mutant shows a redox sensitivity similar to the wild-type enzyme
C413S
O23553, Q9LIR6
site-directed mutagenesis, the mutant shows a redox sensitivity similar to the wild-type enzyme
C470S
O23553, Q9LIR6
site-directed mutagenesis, the mutant shows 70% impaired redox sensitivity compared to the wild-type enzyme
C506S
O23553, Q9LIR6
site-directed mutagenesis, the mutant shows a redox sensitivity similar to the wild-type enzyme
E380Q
-
structural modeling of BAM-9. BAM-4 and BAM-9 are also substituted at position 342 on the inner loop
E172A
-
catalytic site mutant
E172A
-
catalytic site mutant, no hydrolytic activity, no rescue of activity by 2 M azide
E172A/E367A
-
catalytic site double mutant, no hydrolytic activity, no rescue of activity by 2 M azide
S235A
-
binding parameters to raw corn starch, kinetic parameters for the hydrolysis of amylose, 88% of wild-type activity with soluble starch as substrate
S235A/Y249A
-
double mutant, binding parameters to raw corn starch, kinetic parameters for the hydrolysis of amylose, 63% of wild-type activity with soluble starch as substrate
S235A/Y249A/W449F/W495F
-
quadruple mutant, kinetic parameters for the hydrolysis of amylose, 51% of wild-type activity with soluble starch as substrate
T47M/Y164E/T328N
P36924
site-directed mutagenesis, the mutation of Y164 leads to disruption of the hydrogen bonding around the catalytic site, the mutant enzyme shows a shifted pH optimum and a 88% decreased kcat compared to the wild-type enzyme
W449F
-
binding parameters to raw corn starch
W449F/W495F
-
double mutant, binding parameters to raw corn starch, kinetic parameters for the hydrolysis of amylose, 61% of wild-type activity with soluble starch as substrate
W495F
-
binding parameters to raw corn starch
W51F
-
beta-amylase mutant
Y164E
P36924
site-directed mutagenesis, the mutation of Y164 leads to disruption of the hydrogen bonding around the catalytic site, the mutant enzyme shows a shifted pH optimum and a 59% decreased kcat compared to the wild-type enzyme
Y164F
P36924
site-directed mutagenesis, the mutation of Y164 leads to disruption of the hydrogen bonding around the catalytic site, the mutant enzyme shows a shifted pH optimum and a 64% decreased kcat compared to the wild-type enzyme
Y164H
P36924
site-directed mutagenesis, the mutation of Y164 leads to disruption of the hydrogen bonding around the catalytic site, the mutant enzyme shows a shifted pH optimum and a 97% decreased kcat compared to the wild-type enzyme
Y164Q
P36924
site-directed mutagenesis, the mutation of Y164 leads to disruption of the hydrogen bonding around the catalytic site, the mutant enzyme shows a shifted pH optimum and a 83% decreased kcat compared to the wild-type enzyme
Y249A
-
binding parameters to raw corn starch, kinetic parameters for the hydrolysis of amylose, 80% of wild-type activity with soluble starch as substrate
D170Q/L172F/Y173L
-, P06547
site-directed mutagenesis, the mutant shows reduced thermostability at 60C compared to the wild-type enzyme
G48A/A51E
-, P06547
site-directed mutagenesis, the mutant shows increased thermostability at 60C compared to the wild-type enzyme
I74V
-, P06547
site-directed mutagenesis, the mutant shows similar thermostability at 60C as the wild-type enzyme
L135V
-, P06547
site-directed mutagenesis, the mutant shows reduced thermostability at 60C compared to the wild-type enzyme
L172F/Y173L
-, P06547
site-directed mutagenesis, the mutant shows reduced thermostability at 60C compared to the wild-type enzyme
R118Q
-, P06547
site-directed mutagenesis, the mutant shows increased thermostability at 60C compared to the wild-type enzyme
R311P/I312L
-, P06547
site-directed mutagenesis, the mutant shows similar thermostability at 60C as the wild-type enzyme
R311P/I312L/S317A
-, P06547
site-directed mutagenesis, the mutant shows increased thermostability at 60C compared to the wild-type enzyme
S133N/L135V
-, P06547
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
S137T/K138A
-, P06547
site-directed mutagenesis, the mutant shows reduced thermostability at 60C compared to the wild-type enzyme
S317A
-, P06547
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
T116M
-, P06547
site-directed mutagenesis, the mutant shows reduced thermostability at 60C compared to the wild-type enzyme
T116M/R118Q
-, P06547
site-directed mutagenesis, the mutant shows reduced thermostability at 60C compared to the wild-type enzyme
T76V
-, P06547
site-directed mutagenesis, the mutant shows similar thermostability at 60C as the wild-type enzyme
T98K/Y99L/A100V/D101E
-, P06547
site-directed mutagenesis, the mutant shows increased thermostability at 60C compared to the wild-type enzyme
Y72D
-, P06547
site-directed mutagenesis, the mutant shows similar thermostability at 60C as the wild-type enzyme
Y72D/I74V/T76V
-, P06547
site-directed mutagenesis, the mutant shows increased thermostability at 60C compared to the wild-type enzyme
S317A
Bacillus circulans NCIMB 11033
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
-
T116M
Bacillus circulans NCIMB 11033
-
site-directed mutagenesis, the mutant shows reduced thermostability at 60C compared to the wild-type enzyme
-
T76V
Bacillus circulans NCIMB 11033
-
site-directed mutagenesis, the mutant shows similar thermostability at 60C as the wild-type enzyme
-
D53A
-
mutant enzyme shows 13% of the wild-type activity towards maltoheptaose
E178Y
-
kinetic data, 43% of specific activity of wild-type SBA, the pH-optimum of mutant enzyme is shifted to pH 6, the hydrogen bond between Glu-380 and Asn-340 is completely disrupted, mutant SBA structure
E186Q
-
site-directed mutagenesis, mutation of catalytic residue, the mutant shows 16000fold decreased activity compared to the wild-type enzyme
E380Q
-
site-directed mutagenesis, mutation of catalytic residue, the mutant shows 37000fold decreased activity compared to the wild-type enzyme
M51T
-
kinetic data, 11% of specific activity of wild-type SBA, the pH-optimum of mutant enzyme is shifted to pH 6.5, the hydrogen bonds between Glu-380 and Asn-340 and between Glu-380 and Lys-295 are completely disrupted, mutant SBA structure
N340T
-
kinetic data, 32% of specific activity of wild-type SBA, the pH-optimum of mutant enzyme is shifted to pH 6.6, the hydrogen bond between Glu-380 and Asn-340 is completely disrupted, mutant SBA structure
T342A
-
site-directed mutagenesis, structural analysis of mutant active site conformation
T342S
-
site-directed mutagenesis, structural analysis of mutant active site conformation
T342V
-
site-directed mutagenesis, structural analysis of mutant active site conformation
W55R
-
mutant enzyme shows 20% of the wild-type activity towards maltoheptaose
D165E
-
Sd2L mutant
L347S
-
Sd2L mutant, mutation increases the thermostability index T50 by 2.1C by slowing thermal unfolding of enzyme during heating
R115C
-
Sd2L mutant, mutation is responsible for the difference in the kinetic properties of the allelic forms
V233A
-
Sd2L and Sd1 mutant, mutation increases the thermostability index T50 of Sd2L by 1.9C, mutation causes an acceleration of the refolding after heating
V233A/L347S
-
Sd2L double mutation resulting in exactly the same sequence as Sd2H beta-amylase, mutation increases the thermostability index T50 of Sd2L by 4C
E380R
-
structural modeling of the BAM-4 active site predicts an inactive protein. BAM-4 and BAM-9 are also substituted at position 342 on the inner loop
additional information
-
knockout plants of palstidic isozymes BMY6 and BMY8/CT-BMY leads to a starch-excess phenotype in leaves
additional information
O23553
construction of BMY8 knockout plants, and of BMY8 RNAi plants, enzyme induction upon a cold shock leads to starch-dependent maltose accumulation, which can be prevented by RNA interference, phenotype and starch content of recombinant BMY8 RNAi plants, freezing tolerance of recombinant plants, overview
additional information
-
bam1, T-DNA insertion mutation, has no elevated starch levels and no lower nighttime maltose levels than the wild type. Mutant bam2, T-DNA insertion mutation. Mutant bam3, formation of a mutant line via the Arabidopsis TILLING Program, has elevated starch levels and lower nighttime maltose levels than the wild type. Mutant bam4, T-DNA insertion mutation, has elevated starch levels. Double mutant bam1 bam3, more severe phenotype than bam3. Total beta-amylase activity is reduced in leaves of bam1 and bam3 mutants but not in bam2 and bam4 mutants
E367A
-
catalytic site mutant, no hydrolytic activity in the absence of azide, in the presence of 2 M azide the mutant enzyme hydrolyzes maltopentaose at pH 7 and 25C producing maltose, mechanism
additional information
-
mutation of two of the three carbohydrate-binding sites aside from the active site: Site2 in domain B and Site1 in domain C
additional information
P36924
engineering of the enzyme's pH optimum, conversion of the pH optimum from the bacterial type with pH 6.7 to the higher-plant type with pH 5.4, from soybean enzyme, overview
L172F/Y173L/A174E
-, P06547
site-directed mutagenesis, the mutant shows reduced thermostability at 60C compared to the wild-type enzyme
additional information
-, P06547
construction of 18 mutants containing ancestral residues derived from a bacterial, common-ancestral beta-amylase sequence, inferred using a phylogenetic tree composed of higher plant and bacterial amylase sequences. Several of these mutants are more thermostable than that of the wild-type amylase, one mutant has both greater activity and greater thermostability. It is necessary to conserve the residues surrounding an ancestral residue if thermostability is to be improved by the ancestral mutation method
L135V
Bacillus circulans NCIMB 11033
-
site-directed mutagenesis, the mutant shows reduced thermostability at 60C compared to the wild-type enzyme
-
additional information
Bacillus circulans NCIMB 11033
-
construction of 18 mutants containing ancestral residues derived from a bacterial, common-ancestral beta-amylase sequence, inferred using a phylogenetic tree composed of higher plant and bacterial amylase sequences. Several of these mutants are more thermostable than that of the wild-type amylase, one mutant has both greater activity and greater thermostability. It is necessary to conserve the residues surrounding an ancestral residue if thermostability is to be improved by the ancestral mutation method
-
M185L/S295A/I297V/S350P/S351P/Q352D/A376S
-
the mutant enzyme acquires enhanced thermostability, but its function as beta-amylase is unchanged. The mutant is stable at pH-values up to 12.5, while the original recombinant enzyme is unstable at pH-values above pH 9.5
additional information
P16098
generation of different specific deletions at the C-terminal tail and complete deletion of the four C-terminal glycine-rich repeats, complete deletion enhances the thermostability, but the incomplete not, both enhance the substrate binding affinity
additional information
-
Sd1 and Sd2L beta-amylase with a 46 amino acid deletion in the C-terminal tail
V430A
-
Sd2L mutant
additional information
Q6Z5B2, Q6Z5B7
a transposon-induced spontaneous mutation results in low beta-amylase content in rice, overview; a transposon-induced spontaneous mutation results in low beta-amylase content in rice, overview
additional information
-
chloroplast-localized enzyme downregulation by expression of antisense mRNA results in a starch-excess phenotype in leaves compared to wild-type plants
additional information
-
a fusion gene that encodes a polypeptide of 1495 amino acids is constructed from the beta-amylase (BA) gene of Clostridium thermosulfurogenes and trehalose synthase (TS) gene of Thermus thermophilus. The fused gene is overexpressed in Escherichia coli, and a recombinant bifunctional fusion protein with beta-amylase at the N-terminal (BATS) or C-terminal (TSBA) of trehalose synthase having both beta-amylase and trehalose synthase activities with an apparent molecular mass of 164000 Da is obtained. BATS or TSBA catalyzes the sequential reaction in which maltose is formed from starch and then is converted into trehalose. The Km values of the BATS and TSBA fusion enzymes for the reaction from starch to trehalose are smaller than those of an equimolar mixture of BA and TS (BA/TS). The kcat value of BATS approximates that of the BA/TS mixture, but that of TSBA exceedes it. TSBA shows much higher sequential catalytic efficiency than the separately expressed BA/TS mixture. The catalytic efficiency of TSBA or BATS is 3.4 or 2.4times higher, respectively, than that of a mixture of individual enzymes. The thermal stability readings of the recombinant fusion enzymes BATS and TSBA are better than that of the mixture of individual recombinant enzymes
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
nutrition
-
traditional use in the manufacture of infant food and sorghum beer in Burkina Faso
brewing
-
beta-amylase allelic forms have different thermostability and kinetic properties, which critically influence their malting quality, production of barley varieties with better malting quality by genetic engineering
industry
-
the enzyme is important in industrial maltose production
nutrition
P16098
use in the brewing industry
nutrition
-
the enzyme is important in maltose production, and in fermentation processes of food and alcoholic beverages
nutrition
-
possible industrial utility for commercial production of maltose-containing syrups from raw corn starch
nutrition
Paenibacillus polymyxa No. 26-1
-
possible industrial utility for commercial production of maltose-containing syrups from raw corn starch
-
nutrition
Sorghum sp.
-
the knowledge about beta-amylase activities in different Sorghum varieties can be used as markers in selection of varieties for production of food, e.g. of infant porridge
nutrition
-
industrial utility for the production of high maltose syrups from raw or soluble starch at 75C
nutrition
-
beta-amylase may have certain industrial applications, e.g. in the beer industry or in the production of maltose syrup, beta-amylase could be a by-product, in addition to carotenoid pigments, in the fermentation downstream
nutrition
Xanthophyllomyces dendrorhous CECT1690
-
beta-amylase may have certain industrial applications, e.g. in the beer industry or in the production of maltose syrup, beta-amylase could be a by-product, in addition to carotenoid pigments, in the fermentation downstream
-