Information on EC 3.2.1.2 - beta-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

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

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

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

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

mode of action of the exo-amylase

Aspergillus terreus, Brettanomyces naardenensis, Debaryomyces sp., Emericella nidulans, Malbranchea cinnamomea, Myceliophthora sepedonium, Nakazawaea holstii, Phaffia rhodozyma, Saccharomyces cerevisiae, Saccharomyces sp., Syncephalastrum racemosum, Thermomyces lanuginosus, Trichosporon beigelii, Wickerhamomyces anomalus

-

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

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

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

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

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

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

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

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

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

-

hydrolysis of O-glycosyl bond

-

exohydrolysis

-

starch degradation I

-

PWY-842

starch degradation II

-

PWY-6724

Starch and sucrose metabolism

00500

-

Metabolic pathways

01100

-

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.

(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

BAM-5

-

BAM-6

-

BAM-7

-

BAM-8

-

BAM-9

-

BAM1

Q9LIR6

-

BAM1

D0VBH4

isozyme

BAM3

-

catalytically active beta-amylase

BAM3

O23553

-

BAM4

-

catalytically inactive beta-amylase

BCB

-

beta amylase

-

beta-amylase

-

beta-amylase

-

beta-amylase

-

beta-amylase

-

beta-amylase

P10537

-

beta-amylase

-

beta-amylase

Q8U2G5

-

beta-amylase

-

beta-amylase

Xanthophyllomyces dendrorhous CECT1690

-

beta-amylase 1

Q9LIR6

-

beta-amylase I

Q9AVJ8, Q9FUK6

-

beta-amylase1

-

beta-amylase2

-

beta-amylase8

O23553

-

BMY

-

BMY

O23553

-

Glycine max, Hordeum vulgare, Solanum tuberosum

BMY

-

Bmy1

-

Bmy1

Q9AVJ8, Q9FUK6

-

Bmy2

-

Cs-COR018

-

CT-BMY

O23553

-

PF0870

Q8U2G5

gene name

saccharogen amylase

-

saccharogenamylase

-

SBA

-

SBA

-

soybean beta-amylase

Sd1

-

one of three allelic forms of Hordeum beta-amylase

654570, 656797

Sd2H

-

one of three allelic forms of Hordeum beta-amylase

654570, 656797

Sd2L

-

one of three allelic forms of Hordeum beta-amylase

654570, 656797

TCMA

I3ZTN9

-

TCMA

Thermococcus sp. CL1

I3ZTN9

-

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

9000-91-3

-

-

SwissProt

ecotype Col-0

-

ecotype Columbia

-

gene At3g23920/F14O13_11, isozyme TR-BAMY; contains six extrachloroplastic isozymes, and three plastid-targeted isozymes

Q9LIR6

SwissProt

gene At4g170990, isozyme CT-BAMY; contains six extrachlorplastic isozymes, and three plastid-targeted isozymes

O23553

SwissProt

gene dl4575c or At4g170990, putative beta-amylase; ecotype Columbia, gene dl4575c or At4g170990

SwissProt

several isozymes

-

-

-

-

-

-

Uniprot

hyperproductive strain BQ10-S1 SpoIII

208605

-

strains BQ10-S1 and BQ10-S1 SpoII

-

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

677409

-

var. mycoides

136419, 208642, 208645, 655912

-

var. mycoides

654708, 655918, 655927

Uniprot

-

-

-

UniProt

Bacillus circulans NCIMB 11033

-

UniProt

-

-

precursor; strain DSM319

Q9RM92

SwissProt

sensu strictu, NCIB 7581

208617

-

strain B6

654141, 678089, 679812

-

strains: IP 5261, NCIB 8291, NCIB 8508, PZH 53, PZH 493

677409

-

Bacillus megaterium B6

strain B6

654141, 678089, 679812

-

Bacillus megaterium DSM319

precursor; strain DSM319

Brettanomyces naardenensis

Q9RM92

SwissProt

-

-

hedge bindweed, collected in Leuven in winter

SwissProt

-

-

-

-

pearl millet, several cultivars, overview

-

tuberous-rooted chervil

-

-

-

-

-

Debaryomyces sp.

-

-

Dioscorea batatus

cultivar ichoimo

-

Thunb.

-

-

-

Emericella nidulans

strain 45

-

Emericella nidulans

strains 45 and MNU82

-

Emericella nidulans 45

strain 45

-

-

-

-

UniProt

-

208604, 208609

-

-

208594, 208595, 208600, 208611, 208615, 208616, 208637, 208638, 208639, 657200, 666557

-

-

656270, 664104, 666019, 678300

P10538

Uniprot

7 isoenzymes: 1', 1, 2, 3, 4, 5 and 6

-

isolated from soil sample from a salt lake obtained from Yuncheng, China

-

isolated from soil sample from a salt lake obtained from Yuncheng, China

-

Hordeum sp.

17 Hordeum species, some with several suspecies, overview

664483

-

-

208595, 208611, 208620, 208626, 208638, 208643, 208647, 664437, 664674, 664793, 665845, 666557, 692736, 703074

-

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

-

cvs. Morex and Steptoe, 2 isozymes beta-amylase1 and beta-amylase2, i.e. Bmy1 and Bmy2

-

fragment; analysis of coding sequence diversity in the Bmy1 gene on chromosome 4H

681863

Q9AVJ8, Q9FUK6

SwissProt

var. Franklin: Sd1, var. Schooner: Sd2L

Uniprot

variety A 7130

-

variety Triumph and abscisic acid-sensitive barley mutant TL43

Hordeum vulgare subsp. spontaneum

-

-

Hordeum vulgare subsp. vulgare

-

-

-

-

208595, 208596, 208607, 208611, 208619, 208629, 208644

-

-

UniProt

varieties Tainung No. 57 and Chailai

Myceliophthora sepedonium

-

Malbranchea cinnamomea

-

-

Linn. cv. Keitt

-

-

-

L. cv. sonora

-

cv. Nanicao

SwissProt

-

-

-

-

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

Q6Z5B7

SwissProt

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

L. var. Kimmaze

-

L. var. Shinsetsu

-

-

208606, 208646

-

ATCC 8523

-

No. 26-1

-

No. 72

-

strains: NCIB 4747, NCIB 7575, NCIB 8158, NCIB 8524. The most potential beta-amylase producer is the strain NCIB 8524

677409

-

Paenibacillus polymyxa No. 26-1

No. 26-1

-

Paenibacillus polymyxa No. 72

No. 72

-

-

-

-

-

-

-

-

UniProt

-

-

Saccharomyces cerevisiae

-

-

-

-

-

-

-

-

-

-

Sorghum sp.

50 varieties

-

Sorghum sp.

cultivar ICSV 111

-

-

Syncephalastrum racemosum

-

strain RR96

-

Syncephalastrum racemosum RR96

strain RR96

-

-

208601, 208602, 208608, 680294

-

-

UniProt

-

UniProt

Thermomyces lanuginosus

-

-

Trichosporon beigelii

-

-

-

208595, 208620, 208630

-

cv. Yangmai 158, isozymes type I and type II

-

-

-

Wickerhamomyces anomalus

-

-

strain CECT1690, the perfect state of Phaffia rhodozyma

-

Xanthophyllomyces dendrorhous CECT1690

strain CECT1690, the perfect state of Phaffia rhodozyma

-

Zea mays

-

681063

-

No entries in this field

4-nitrophenyl alpha-D-galactoside + H2O

4-nitrophenol + D-galactose

-, Q8U2G5

-

-

?

4-nitrophenyl alpha-maltopyranoside + H2O

4-nitrophenol + alpha-maltopyranose

-, Q8U2G5

-

-

?

4-nitrophenyl maltopentaose + H2O

4-nitrophenol + maltopentaose

O23553, Q9LIR6

-

-

?

4-nitrophenyl-maltoheptaoside + H2O

?

-

-

?

4-nitrophenyl-maltopentaoside + H2O

?

-

-

?

alpha-glucan + H2O

?

Musa acuminata

Q3S4X4

-

682492

-

?

amylopectin + H2O

maltose + ?

-

-

?

amylopectin + H2O

maltose + ?

P36924

-

-

?

amylopectin + H2O

maltose + ?

-, Q9FQ07

catalyzes the release of maltose residues, amylopectin and starch are better substrates than amylose

-

?

amylopectin + H2O

maltose + ?

Sorghum sp.

-

from starch, preferred substrate

-

?

amylopectin + H2O

maltose + ?

-

from potato

664104, 666019

-

?

amylopectin + H2O

maltose + ?

P36924

from potato

-

?

amylopectin + H2O

maltose + ?

I3ZTN9

the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan

-

?

amylopectin + H2O

?

-

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

?

-

88% of the activity with starch

-

?

amylopectin + H2O

?

P10538

from potato, active site structure, Glu-186 and Glu-380 play important roles as general acid and base catalyst

-

?

amylopectin + H2O

?

Bacillus megaterium B6

-

88% of the activity with starch

-

?

amylopectin + H2O

beta-maltose + ?

-

-

?

amylopectin + H2O

beta-maltose + ?

-

-

?

amylopectin + H2O

beta-maltose + ?

-

-

?

amylopectin + H2O

beta-maltose + ?

-

208614, 208638

-

?

amylopectin + H2O

beta-maltose + ?

-

-

?

amylopectin + H2O

beta-maltose + ?

-

-

?

amylopectin + H2O

beta-maltose + ?

-

-

?

amylopectin + H2O

beta-maltose + ?

-

-

?

amylopectin + H2O

beta-maltose + ?

-

-

?

amylopectin + H2O

beta-maltose + ?

-

-

?

amylopectin + H2O

beta-maltose + ?

-

-

?

amylopectin + H2O

beta-maltose + ?

-

-

?

amylopectin + H2O

beta-maltose + ?

-

-

?

amylopectin + H2O

beta-maltose + ?

-

and limit dextrin

?

amylopectin + H2O

beta-maltose + ?

Paenibacillus polymyxa No. 26-1

-

-

?

amylose + H2O

?

-

79% of the activity with starch

-

?

amylose + H2O

?

-

DPn is 16

-

?

amylose + H2O

?

-

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

?

Bacillus megaterium B6

-

79% of the activity with starch

-

?

amylose + H2O

beta-maltose

-

-

?

amylose + H2O

beta-maltose

-

703074

-

?

amylose + H2O

beta-maltose

-

-

?

amylose + H2O

beta-maltose

-

-

?

amylose + H2O

beta-maltose

-

-

?

amylose + H2O

beta-maltose

-

-

?

amylose + H2O

beta-maltose

-

-

?

amylose + H2O

beta-maltose

-

-

?

amylose + H2O

beta-maltose

-

-

?

amylose + H2O

beta-maltose

-

-

?

amylose + H2O

beta-maltose

-

-

?

amylose + H2O

beta-maltose

-

-

?

amylose + H2O

beta-maltose

-

partly oxidized amylose

-

?

amylose + H2O

beta-maltose

-

DP = 17

-

?

amylose + H2O

beta-maltose

Paenibacillus polymyxa No. 26-1

-

-

?

amylose + H2O

maltose + ?

-, Q9FQ07

catalyzes the release of maltose residues, less good substrate than starch and amylopectin

-

?

amylose + H2O

maltose

Sorghum sp.

-

from starch

-

?

dextrin + H2O

?

-

-

?

dextrin + H2O

?

Bacillus megaterium, Bacillus megaterium B6

-

13% of the activity with starch

-

?

glycogen + H2O

?

-

49.4% of the activity with amylose

-

?

glycogen + H2O

?

-, Q8U2G5

the enzyme is specific for short alpha-glucans. Similar responses to maltose, glycogen, and starch but not to pullulan

-

?

glycogen + H2O

beta-maltose

-

-

?

glycogen + H2O

beta-maltose

-

-

?

glycogen + H2O

beta-maltose

-

-

?

glycogen + H2O

beta-maltose

-

-

?

glycogen + H2O

beta-maltose

-

and limit dextrin

?

glycogen + H2O

beta-maltose

-

from oyster

-

?

glycogen + H2O

beta-maltose

-

type III and type VIII

-

?

glycogen + H2O

maltose + ?

I3ZTN9

the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan

-

?

maltal + H2O

2-deoxymaltose

-

208607

-

208607

?

maltodextrin + H2O

maltose

-

maltodextrins with chain length from 9 to 198 glucose residues

and very small amounts of glucose and maltotriose

?

maltoheptaose + H2O

?

-

-

?

maltoheptaose + H2O

?

-

-

?

maltoheptaose + H2O

?

-

-

?

maltoheptaose + H2O

?

-

34.6% of the activity with amylose

-

?

maltoheptaose + H2O

maltose

-

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

?

-

-

?

maltohexaose + H2O

?

-

-

?

maltohexaose + H2O

?

-

23.3% of the activity with amylose

-

?

maltooligosaccharide + H2O

?

-

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

?

-

-

?

maltopentaose + H2O

?

-

-

?

maltopentaose + H2O

?

-

13.8% of the activity with amylose

-

?

maltopentaose + H2O

?

-

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

?

-

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

?

-

binding mode of substrate in the active site

-

?

maltopentaose + H2O

?

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

-

substrate/product binding structure, sugar subsite conformations, overview

-

?

maltopentaose + H2O

2 maltose + D-glucose

I3ZTN9

the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible

-

?

maltopentose + H2O

?

Xanthophyllomyces dendrorhous, Xanthophyllomyces dendrorhous CECT1690

-

40% of the activity with starch, exo-acting enzyme, no production of glucose

-

?

maltose + H2O

?

-, Q8U2G5

the enzyme is specific for short alpha-glucans. Similar responses to maltose, glycogen, and starch but not to pullulan

-

?

maltotetraose + H2O

?

-

-

?

maltotetraose + H2O

?

-

-

?

maltotetraose + H2O

?

-

37% of the activity with starch, exo-acting enzyme, no production of glucose

-

?

maltotetraose + H2O

?

-

7.6% of the activity with amylose

-

?

maltotetraose + H2O

?

Xanthophyllomyces dendrorhous CECT1690

-

37% of the activity with starch, exo-acting enzyme, no production of glucose

-

?

maltotetraose + H2O

2 maltose

I3ZTN9

the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible

-

?

maltotriose + H2O

?

-

very poor substrate

-

?

p-nitrophenyl-alpha-D-glucopyranoside + H2O

p-nitrophenol + glucose

-

-

?

p-nitrophenylmaltopentaoside + H2O

?

-

-

?

p-nitrophenylmaltopentaoside + H2O

?

-

-

?

p-nitrophenylmaltopentaoside + H2O

?

P16098

catalyzes the release of maltose

-

?

p-nitrophenylmaltopentaoside + H2O

?

-

catalyzes the release of maltose

-

?

p-nitrophenylmaltopentaoside + H2O

p-nitrophenol + maltopentaose

-, Q9FQ07

catalyzes the release of p-nitrophenol, specific substrate

-

?

pullulan + H2O

?

-

-

?

soluble starch + H2O

?

-

-

?

soluble starch + H2O

?

-

starch granules from various sources

-

?

soluble starch + H2O

maltose + ?

I3ZTN9

the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan

-

?

starch + H2O

?

Saccharomyces cerevisiae, Emericella nidulans, Nakazawaea holstii, Phaffia rhodozyma, Aspergillus terreus, Saccharomyces sp., Wickerhamomyces anomalus, Thermomyces lanuginosus, Syncephalastrum racemosum, Malbranchea cinnamomea, Trichosporon beigelii, Brettanomyces naardenensis, Myceliophthora sepedonium, Debaryomyces sp.

-

-

?

starch + H2O

?

-

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

?

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

?

-

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 45°C

-

?

starch + H2O

?

-

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

?

-

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

?

-

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

?

-

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

?

-

catalyzes the release of maltose from soluble starch, three-dimensional structures of Sd2L and V233A mutant of Sd1

-

?

starch + H2O

?

P16098

from potato, catalyzes the release of maltose from the non-reducing ends of starch, three-dimensional structure of Sd2L

-

?

starch + H2O

?

-

highest activity, exo-acting enzyme, no production of glucose

-

?

starch + H2O

?

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

?

Saccharomyces cerevisiae, Nakazawaea holstii, Phaffia rhodozyma, Aspergillus terreus, Saccharomyces sp., Wickerhamomyces anomalus, Thermomyces lanuginosus, Syncephalastrum racemosum, Malbranchea cinnamomea, Trichosporon beigelii, Brettanomyces naardenensis, Myceliophthora sepedonium, Debaryomyces sp.

-

starch substrate of different sources, e.g. wheat, wheat bran, rice bran

-

?

starch + H2O

?

Emericella nidulans

-

starch substrate of different sources, e.g. wheat, wheat bran, rice bran, the enzyme from strain MNU82 utilizes raw and cooked starch

-

?

starch + H2O

?

O23553, Q9LIR6

in vitro breakdown of semicrystalline starch particles by beta-amylases increases significantly if they act together with glucan, water dikinase

-

?

starch + H2O

?

-, Q8U2G5

the enzyme is specific for short alpha-glucans. Similar responses to maltose, glycogen, and starch but not to pullulan

-

?

starch + H2O

?

Xanthophyllomyces dendrorhous CECT1690

-

highest activity, exo-acting enzyme, no production of glucose

-

?

starch + H2O

?

Syncephalastrum racemosum RR96

-

-, starch substrate of different sources, e.g. wheat, wheat bran, rice bran

-

?

starch + H2O

maltose

-

-

?

starch + H2O

maltose

-

-

?

starch + H2O

maltose

-

-

?

starch + H2O

maltose

Solanum tuberosum, Glycine max, Arabidopsis thaliana

-

664437, 703047, 703074, 706275

-

?

starch + H2O

maltose

-

-

?

starch + H2O

maltose

-

-

?

starch + H2O

maltose

-

-

?

starch + H2O

maltose

-

-

?

starch + H2O

maltose

Secale cereale

-

-

?

starch + H2O

maltose

Sorghum sp.

-

-

?

starch + H2O

maltose

-

-

?

starch + H2O

maltose

O23553

-

666599, 666646

-

?

starch + H2O

maltose

Q9LIR6

-

-

?

starch + H2O

maltose

-

-

?

starch + H2O

maltose

D0VBH4, -

-

-

?

starch + H2O

maltose

-

beta-maltose

?

starch + H2O

maltose

-

soluble

-

?

starch + H2O

maltose

-

soluble

-

?

starch + H2O

maltose

-

soluble

-

?

starch + H2O

maltose

-

soluble

-

?

starch + H2O

maltose

-

soluble

-

?

starch + H2O

maltose

-

soluble

-

?

starch + H2O

maltose

-

soluble

-

?

starch + H2O

maltose

-

soluble

-

?

starch + H2O

maltose

-

soluble

208606, 208641

-

?

starch + H2O

maltose

-

soluble

208601, 208602

-

?

starch + H2O

maltose

-

soluble

-

?

starch + H2O

maltose

-

soluble

-

?

starch + H2O

maltose

-

soluble

-

?

starch + H2O

maltose

-

soluble

-

?

starch + H2O

maltose

-

soluble

beta-maltose

?

starch + H2O

maltose

-

soluble

208612

beta-maltose

208612

?

starch + H2O

maltose

-

soluble

beta-maltose

?

starch + H2O

maltose

Dioscorea batatus

-

soluble

beta-maltose

?

starch + H2O

maltose

-

soluble starch

-

?

starch + H2O

maltose

O23553, Q9LIR6

soluble starch

-

?

starch + H2O

maltose

-

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

-

potato starch

-

?

starch + H2O

maltose

-

potato starch

-

?

starch + H2O

maltose

-

raw starch from wheat, corn, potato and rice

-

?

starch + H2O

maltose

-

gelatinized starch

-

?

starch + H2O

maltose

-

boiled

-

?

starch + H2O

maltose

-

grains

-

starch + H2O

maltose

O23553

enzyme induction upon a cold shock at 4°C 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

-

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

-

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

O23553, Q9LIR6

the isozyme is involved in leaf starch degradation

-

?

starch + H2O

maltose

-

millet starch, gelatinization temperature is 61.1-68.7°C

-

?

starch + H2O

maltose

-

soluble starch, depolymerization, reaction scheme

-

?

starch + H2O

maltose

Sorghum sp.

-

Sorghum starch, gelatinization temperature is 70-75°C

-

?

starch + H2O

maltose

-

waxy from maize

-

?

starch + H2O

maltose

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

Bacillus megaterium B6

-

-

?

starch + H2O

maltose

Paenibacillus polymyxa No. 72

-

beta-maltose

?

starch + H2O

beta-maltose

-

692736

-

?

starch + H2O

beta-maltose

-

-

?

starch + H2O

beta-maltose

P10537

-

-

?

starch + H2O

beta-maltose

-

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

Mangifera indica

-

beta-amylase is involved in starch degradation during mango ripening, which is clearly triggered by detachment from the mother-plant

692730

-

?

starch + H2O

beta-maltose

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 + ?

-

-

?

starch + H2O

maltose + ?

Q9RM92

-

-

?

starch + H2O

maltose + ?

-, Q9FQ07

catalyzes the release of maltose residues, starch and amylopectin are better substrates than amylose

-

?

starch + H2O

maltose + ?

Bacillus megaterium DSM319

Q9RM92

-

-

?

starch + H2O

beta-maltose + ?

-

-

?

maltotriose + H2O

maltose + D-glucose

I3ZTN9

the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible

-

?

additional information

?

-

-

-

additional information

?

-

-

soybean trypsin inhibitor and beta-amylase induce rat alveolar macrophages to release nitrogen oxides

208639

-

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

208606

-

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

Hordeum vulgare, Secale cereale

-

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

703047

-

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

-

amylopectin + H2O

maltose + ?

-

-

?

amylopectin + H2O

maltose + ?

P36924

-

-

?

amylopectin + H2O

maltose + ?

Sorghum sp.

-

from starch, preferred substrate

-

?

amylopectin + H2O

beta-maltose + ?

-

-

?

amylose + H2O

maltose

Sorghum sp.

-

from starch

-

?

starch + H2O

?

Saccharomyces cerevisiae, Emericella nidulans, Nakazawaea holstii, Phaffia rhodozyma, Aspergillus terreus, Saccharomyces sp., Wickerhamomyces anomalus, Thermomyces lanuginosus, Syncephalastrum racemosum, Malbranchea cinnamomea, Trichosporon beigelii, Brettanomyces naardenensis, Myceliophthora sepedonium, Debaryomyces sp.

-

-

?

starch + H2O

?

-

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

-

-

?

starch + H2O

maltose

Solanum tuberosum, Glycine max

-

664437, 706275

-

?

starch + H2O

maltose

-

-

?

starch + H2O

maltose

Sorghum sp.

-

-

?

starch + H2O

maltose

O23553, Q9LIR6

-

-

?

starch + H2O

maltose

-

-

?

starch + H2O

maltose

D0VBH4, -

-

-

?

starch + H2O

maltose

O23553

enzyme induction upon a cold shock at 4°C 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

-

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

-

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

O23553, Q9LIR6

the isozyme is involved in leaf starch degradation

-

?

starch + H2O

beta-maltose

-

692736

-

?

starch + H2O

beta-maltose

-

-

?

starch + H2O

beta-maltose

P10537

-

-

?

starch + H2O

beta-maltose

Mangifera indica

-

beta-amylase is involved in starch degradation during mango ripening, which is clearly triggered by detachment from the mother-plant

692730

-

?

starch + H2O

?

Syncephalastrum racemosum RR96

-

-

?

maltotetraose + H2O

?

-

-

?

additional information

?

-

-

Hordeum vulgare, Secale cereale

-

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

Halobacillus sp., Halobacillus sp. LY9

-

additional information

?

-

-

maltose is the main product of soluble starch hydrolysis

-

No entries in this field

2-mercaptoethanol

-

activates

Ba2+

-

stimulates

BaCl2

-

1 mM, activates

Ca2+

-

stimulates

Ca2+

-

100 mM CaCl2, 29% stimulation

Ca2+

Syncephalastrum racemosum

-

one Ca2+ is bound per molecule of enzyme far from the active site

208645

Ca2+

-

activates

Ca2+

-

activates

CaCl2

-

1 mM, activates

CoCl2

-

1 mM, activates

cysteine

-

activates

dithiothreitol

-

activates

K+

-

stimulates

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

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

Emericella nidulans

-

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+

-

Ag+

-

0.001-0.1 mM AgNO3

Ag+

-

Ag+

-

AgNO3

Ag+

-

AgNO3

Ag+

-

1 mM, almost complete inhibition of mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S

Ag+

-

0.5 mM

Ag+

-

1 mM, almost complete inhibition of recombinant enzyme

Ag+

-

Ag2+

-

AgNO3

-

1 mM, 94% inhibition

Al2(SO4)3

-

1 mM, 57% inhibition

Al3+

-

mild inhibitor

alpha-cyclodextrin

Bacillus circulans, Bacillus megaterium, Glycine max, Hordeum vulgare, Ipomoea batatas

-

alpha-cyclodextrin

-

alpha-cyclodextrin

-

alpha-cyclohexaamylose

-

Aprotinin

-

beta-amylase-inhibitor

-

several strains of Streptomyces produce a beta-amylase inhibitor when grown on a medium containing starch and deoxynojirimycin

208611

-

beta-cyclodextrin

-

beta-cyclodextrin

-

Bi(NO3)3

-

1 mM, 54% inhibition

Ca2+

-

binds at the active site

Cd2+

-

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

CO32-

-

Cu2+

-

Cu2+

-

Cu2+

-

1 mM CuSO4, 50% inhibition

Cu2+

-

Cu2+

-

CuCl2

Cu2+

-

Cu2+

-

CuSO4

Cu2+

-

1 mM, almost complete inhibition of mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S

Cu2+

-

0.5 mM

Cu2+

-

1 mM, almost complete inhibition of recombinant enzyme

Cu2+

-

5 mM, 37°C, 30 min, about 80% inhibition

Cu2+

-

Cu2+

-

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

DTNB

-

EDTA

-

non-competitive

EDTA

-

non-competitive, Ca2+ fully restores activity

EDTA

-

EDTA

-

EGTA

-

Fe2+

-

Fe3+

-

Fe3+

-

FeCl3

-

1 mM, 16% inhibition

H2O2

-

weak

Hg2+

-

HgCl2

Hg2+

-

Hg2+

-

0.001-0.1 mM HgCl2

Hg2+

-

Hg2+

-

Hg2+

-

Hg2+

-

HgCl2

Hg2+

-

HgCl2

Hg2+

-

Hg2+

-

1 mM, almost complete inhibition of mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S

Hg2+

-

0.5 mM

Hg2+

-

1 mM, almost complete inhibition of recombinant enzyme

Hg2+

-

5 mM, 37°C, 30 min, about 80% inhibition

Hg2+

-

Hg2+

-

HgCl2

-

1 mM, 93% inhibition

HgCl2

-

10 mM, 100% inhibition

iodoacetamide

-

iodoacetamide

-

iodoacetamide

-

iodoacetic acid

-

partial

iodoacetic acid

-

iodoacetic acid

-

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+

-

mild inhibitor

Mg2+

-

binds at the active site

Mn2+

-

mild inhibitor

N-bromosuccinimide

-

0.4 mM

N-bromosuccinimide

-

1 mM, 84% inhibition

N-ethylmaleimide

-

remarkably reduces activity

N-ethylmaleimide

-

10 mM, 73% inhibition

N-ethylmalimide

-

NaCN

-

0.1%

NaNO2

-

partial

NEM

-

NEM

-

partial

NEM

-

weak

NEM

-

NEM

-

Ni2+

-

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

Pb2+

-

PCMB

-

cysteine reactivates

PCMB

-

PCMB

-

0.001-0.1 mM, inactivation is partly reversed by adding 10fold to 20fold excess of glutathione or 1,2-dithiopropanol

PCMB

-

PCMB

-

208601, 208602, 208608

PCMB

-

208604, 208609

PCMB

-

5 nM

PCMB

-

0.5 mM, 75% loss of activity after 30 min at 22°C, cysteine reactivates

208617

PCMB

-

cysteine reactivates

PCMB

-

PCMB

-

restored by mercaptoethanol or dithiothreitol

PCMB

-

PCMB

-

PCMB

-

PCMB

-

208595, 208616, 208638

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

PMSF

-

2 mM

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

Urea

-

Zn2+

-

mild inhibitor

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

Zn2+

-

ZnSO4

-

1 mM, 54% inhibition

Mn2+

-

5 mM, 37°C, 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

Syncephalastrum racemosum

-

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

-

2-mercaptoethanol

-

1 mM, activates

CaCl2

-

NaCl

-

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

Triton X-100

-

Triton X-114

-

MgCl2

-

additional information

-

the synthesis of beta-amylase is induced by starch and maltose

-

additional information

-

low temperature of 4°C rapidly induces the enzyme activity

-

additional information

-

cold stress activates the chloroplastic isozyme by 5fold at 3°C

-

additional information

O23553

the enzyme is induced during low temperature stress at 4°C

-

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

-

0.0827

-

4-nitrophenyl alpha-maltopyranoside

-, Q8U2G5

pH 7.0, 90°C

-

0.13

0.17

amylodextrin

-

chain lengths geater than 50

-

0.26

-

Amylopectin

-

pH 5.4, 37°C, recombinant mutant T342A

0.39

-

Amylopectin

-

pH 5.4, 37°C, recombinant mutant T342S

0.47

-

Amylopectin

P36924

37°C, recombinant mutant T47M/Y164E/T328N

0.73

-

Amylopectin

P36924

37°C, recombinant wild-type enzyme

0.92

-

Amylopectin

P36924

37°C, recombinant mutant Y164F

1.22

-

Amylopectin

P36924

37°C, recombinant mutant Y164Q

1.24

-

Amylopectin

P36924

37°C, recombinant mutant Y164E

1.84

-

Amylopectin

-

pH 5.4, 37°C, recombinant mutant T342V

1.94

-

Amylopectin

-

pH 5.4, 37°C, recombinant wild-type enzyme

2.63

-

Amylopectin

P36924

37°C, recombinant mutant Y164H

0.491

-

Amylose

-

DP = 17, mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S

0.6

-

Amylose

-

pH 7, 25°C, DPn: 16, S235A/Y249A/W449F/W495F quadruple mutant

0.61

-

Amylose

-

pH 7, 25°C, DPn: 16, W449F/W495F double mutant

0.65

-

Amylose

-

pH 7, 25°C, DPn: 16, S235A/Y249A double mutant

0.7

-

Amylose

-

pH 7, 25°C, DPn: 16, S235A mutant

0.71

-

Amylose

-

pH 7, 25°C, DPn: 16, Y249A mutant

0.72

-

Amylose

-

pH 7, 25°C, DPn: 16, wild-type enzyme

94.5

-

maltal

-

208607

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, 37°C, wild-type enzyme

2.02

-

maltopentaose

-

pH 5.4, 37°C, mutant E380Q

2.15

-

maltopentaose

-

pH 5.4, 37°C, mutant E186Q

2.83

-

maltopentaose

-

mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S

16.2

-

maltopentaose

I3ZTN9

pH 5.0, 85°C

4.17

-

maltotetraose

-

mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S

18.2

-

maltotetraose

I3ZTN9

pH 5.0, 85°C

0.73

-

p-nitrophenylmaltopentaoside

-

0.00317

-

starch

-

pH 5, 40°C, soluble starch, V233A mutant of Sd1

0.0033

-

starch

-

pH 5, 40°C, soluble starch, wild-type Sd1

0.0036

-

starch

-

pH 5, 40°C, soluble starch, R115C mutant of Sd2L

0.00825

-

starch

-

pH 5, 40°C, soluble starch, V233A mutant of Sd2L

0.0083

-

starch

-

pH 5, 40°C, soluble starch, wild-type Sd2H and V233A/L347S double mutant of Sd2L

0.00831

-

starch

-

pH 5, 40°C, soluble starch, wild-type Sd2L

0.00834

-

starch

-

pH 5, 40°C, soluble starch, L347S mutant of Sd2L

0.00838

-

starch

-

pH 5, 40°C, soluble starch, V430A mutant of Sd2L

0.00856

-

starch

-

pH 5, 40°C, soluble starch, D165E mutant of Sd2L

0.77

-

starch

-

soluble

4.25

-

maltotriose

I3ZTN9

pH 5.0, 85°C

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 60°C, 1.68 mg/ml for soluble starch at 75°C

-

additional information

-

additional information

-

Km: 1.25 mg/ml for starch

-

additional information

-

additional information

-

208609

-

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

Pyrus communis

-

208625

-

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 60°C

-

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

-

962

-

4-nitrophenyl alpha-maltopyranoside

-, Q8U2G5

pH 7.0, 90°C

-

0.24

-

Amylopectin

-

pH 5.4, 37°C, recombinant mutant T342V

0.75

-

Amylopectin

-

pH 5.4, 37°C, recombinant mutant T342A

3.5

-

Amylopectin

-

pH 5.4, 37°C, recombinant mutant T342S

92

-

Amylopectin

P36924

37°C, recombinant mutant Y164H

98.4

-

Amylopectin

-

pH 5.4, 37°C, recombinant mutant T342V

325

-

Amylopectin

P36924

37°C, recombinant mutant T47M/Y164E/T328N

453

-

Amylopectin

P36924

37°C, recombinant mutant Y164Q

550

-

Amylopectin

-

988

-

Amylopectin

P36924

37°C, recombinant mutant Y164F

1129

-

Amylopectin

P36924

37°C, recombinant mutant Y164E

1280

-

Amylopectin

-

pH 5.4, 37°C, recombinant wild-type enzyme

2739

-

Amylopectin

P36924

37°C, recombinant wild-type enzyme

2400

-

Amylose

-

0.034

-

maltopentaose

-

pH 5.4, 37°C, mutant E380Q

0.08

-

maltopentaose

-

pH 5.4, 37°C, mutant E186Q

3.85

-

maltopentaose

I3ZTN9

pH 5.0, 85°C

1280

-

maltopentaose

-

pH 5.4, 37°C, wild-type enzyme

3.95

-

maltotetraose

I3ZTN9

pH 5.0, 85°C

299

-

starch

-

pH 5, 40°C, soluble starch, wild-type Sd2L

305

-

starch

-

pH 5, 40°C, soluble starch, wild-type Sd1

308

-

starch

-

pH 5, 40°C, soluble starch, wild-type Sd2H and V233A/L347S double mutant of Sd2L

309

-

starch

-

pH 5, 40°C, soluble starch, L347S and R115C mutants of Sd2L

314

-

starch

-

pH 5, 40°C, soluble starch, V233A mutant of Sd1

315

-

starch

-

pH 5, 40°C, soluble starch, V233A mutant of Sd2L

319

-

starch

-

pH 5, 40°C, 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

11.45

-

maltotriose

I3ZTN9

pH 5.0, 85°C

additional information

-

additional information

-

-

additional information

-

additional information

-

-

additional information

-

additional information

P16098

kinetic parameters for several deletion mutants

-

additional information

-

additional information

-

-

0.24

-

maltopentaose

I3ZTN9

pH 5.0, 85°C

272

0.22

-

maltotetraose

I3ZTN9

pH 5.0, 85°C

269

2.7

-

maltotriose

I3ZTN9

pH 5.0, 85°C

188

13.1

13.4

Ca2+

-

pH 4.8, 27°C

0.36

-

cyclohexaamylose

-, Q9FQ07

pH 5, 20°C, iodine staining method

0.8

-

cyclohexaamylose

-

pH 7, 25°C, wild-type enzyme, amylose as substrate

262

-

D-glucose

-, Q9FQ07

pH 5, 20°C, iodine staining method

11.7

-

D-maltose

-, Q9FQ07

pH 5, 20°C, iodine staining method

2.8

-

maltitol

-

pH 7, 25°C, wild-type enzyme, amylose as substrate

3.1

-

maltitol

-

pH 7, 25°C, wild-type enzyme, maltopentaose as substrate

5.1

-

maltitol

-

pH 7, 25°C, S235A/Y249A double mutant, amylose as substrate

5.7

-

maltitol

-

pH 7, 25°C, 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, 25°C, wild-type enzyme, amylose as substrate

17.5

17.7

Zn2+

-

pH 4.8, 27°C

18.6

-

Mg2+

-

pH 4.8, 27°C

additional information

-

additional information

-

inhibition kinetics

-

No entries in this field

0.0685

-

-

pH 5.5, 50°C

0.45

-

Wickerhamomyces anomalus

-

0.475

-

Nakazawaea holstii

-

5

-

-

45.95

-

Sorghum sp.

-

96 h germination, the enzyme activity increases progressively during seed germination, overview

65.1

-

-

100

-

-

103.9

-

-

pH 4.5, 37°C, soluble starch

161

-

Dioscorea batatus

-

222

-

-

208626

300

-

-

508.3

-

-

561

-

-

986

-

P10537

A-7005; type I-B

1030

-

-

1077

-

-

1187

-

-

208600

1500

-

-

4215

-

-

4464

-

-

variant Tainung No.57

4664

-

-

variant Chailai

additional information

-

-

additional information

-

-

additional information

-

-

additional information

-

-

isoenzyme 6

additional information

-

-

additional information

-

-

additional information

-

Pyrus communis

-

208625

additional information

-

-

additional information

-

-

additional information

-

-

additional information

-

-

Aspergillus terreus, Brettanomyces naardenensis

additional information

-

-

additional information

-

Emericella nidulans

-

strain 45

Malbranchea cinnamomea, Myceliophthora sepedonium, Phaffia rhodozyma, Saccharomyces cerevisiae, Syncephalastrum racemosum, Thermomyces lanuginosus, Trichosporon beigelii

additional information

-

-

additional information

-

-

catalytic activity of the enzyme at different pressure/temperature conditions, up to 700 mPa, 20-70°C, 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

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

-

-

5

-

-

5

-

P16098

assay at, potato starch as substrate

5

-

-

assay at, starch as substrate

Brettanomyces naardenensis, Syncephalastrum racemosum

5

-

-

5

-

I3ZTN9

alpha-1,4-glycosidic linkage hydrolysis

5.3

-

-

5.4

6

-

5.4

-

-

isoenzyme 2 and 6

5.4

-

-

hydrolysis of potato amylopectin, at 37°C, 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

6

-

5.5

6.5

-

5.5

7

Emericella nidulans

-

enzyme from strain 45

5.5

-

-

5.5

-

-

native enzyme

5.5

-

-

degradation of glycogen

5.5

-

-

raw corn starch

5.5

-

-

5.6

-

-

5.6

-

-

6

7

-

6

8

O23553, Q9LIR6

-

Glycine max, Ipomoea batatas

6

-

-

6

-

-

6

-

-

6

-

-

immobilized enzyme

6

-

-

6

-

Dioscorea batatus

-

6

-

Phaffia rhodozyma

-

6

-

P36924

mutant T47M/Y164E/T328N

6

-

-

assay at

6

-

-

assay at, phosphate buffer

6

-

I3ZTN9

alpha-1,6-glycosidic linkage hydrolysis

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

-

Emericella nidulans

-

enzyme from strain MNU82

6.7

-

P36924

wild-type enzyme

6.9

-

-

6.9

-

-

7

7.5

Emericella nidulans

-

7

-

-

7

-

-

7

-

-

7

-

-

assay at

655912, 655927

7

-

-

assay at

7

-

-

7.5

-

-

7.5

-

Q9RM92

-

7.5

-

-, P06547

assay at

8

-

-

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

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

I3ZTN9

pH 4.0: about 85% of maximal activity, pH 6.0: about 60% of maximal activity, alpha-1,4-glycosidic linkage hydrolysis of maltotriose

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

8

I3ZTN9

pH 4.0: about 50% of maximal activity, pH 8.0: about 70% of maximal activity, alpha-1,6-glycosidic linkage hydrolysis of 6-O-maltotetraosyl-beta-cyclodextrin

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

Emericella nidulans

-

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

4

-

-

higher activity of beta-amylase at 4°C compared to 10-16 °C

20

-

-, Q9FQ07

assay at, starch, amylose or amylopectin as substrate

25

-

-

assay at

655912, 655927

25

-

Cenchrus sp., Sorghum sp.

-

assay at

25

-

-

assay at

25

-

P10537

assay at

27

-

-

assay at

30

40

-

Bacillus cereus, Glycine max

35

-

-

assay at

37

-

P36924

assay at

37

-

-

assay at

37

-

-

assay at

37

-

-

assay at

37

-

O23553, Q9LIR6

assay at

40

-

-

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

-

-

45

-

-

raw corn starch

45

-

-

50

55

-

50

-

-

50

-

-

208598

50

-

-

50

-

-

native enzyme

50

-

-

50

-

-

gelatinized starch

50

-

-

50

-

Q9RM92

-

55

-

-

immobilized enzyme

55

-

Dioscorea batatus

-

55

-

-

55

-

-

original and recombinant enzyme

55

-

-

55

-

-

optimum temperature after 30 min incubation

55

-

-

approximately

60

-

Emericella nidulans

-

60

-

-

60

-

-

temperature optimum, but enzyme loses activity when exposed to 60°C, irreversible thermodenaturation

60

-

Emericella nidulans, Syncephalastrum racemosum

-

60

-

-

65

-

-

mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S

70

-

-

native immobilized beta-amylase

75

-

-

75

-

-

hydrolysis of gelatinized starch

75

-

-

75

-

-

chemically modified and subsequently immobilized beta-amylase

80

-

-

85

-

I3ZTN9

alpha-1,4-glycosidic linkage hydrolysis

98

-

I3ZTN9

alpha-1,6-glycosidic linkage hydrolysis

20

60

-

active in the range

20

70

-

at different pressure/temperature conditions, up to 700 mPa, overview

28

61

-

28°C: about 40% of maximal activity, 61°C: about 30% of maximal activity

29

41

-

75% of maximal activity at 29°C and at 41°C

30

60

-

30°C: about 25% of maximal activity, 60°C: about 20% of maximal activity, hyrolysis of raw corn starch

40

60

Dioscorea batatus

-

40°C: about 30% of maximal activity, 60°C: about 50% of maximal activity

45

-

-

beta-amylase hydrolyzes corn starch granules efficiently at 45°C, 60% more active than soybean beta-amylase at 45°C

45

-

-

at 45°C beta-amylase is 60% less active in hydrolysis of corn starch granules than enzyme from Bacillus cereus

50

70

Emericella nidulans

-

50°C: about 55% of maximal activity, 70°C: about 70% of maximal activity

50

70

-

activity range

50

80

-

50°C: about 55% of maximal activity, 80°C: about 65% of maximal activity

50

85

-

50°C: about 45% of maximal activity, 85°C: about 25% of maximal activity

60

95

I3ZTN9

60°C; about 50% of maximal activity, 60°C: about 60% of maximal activity, alpha-1,4-glycosidic linkage hydrolysis of maltotriose

80

98

I3ZTN9

activity at 80°C is about 50% compared to the activity at 98°C, alpha-1,6-glycosidic linkage hydrolysis of 6-O-maltotetraosyl-beta-cyclodextrin

85

90

-

85°C: 83% of maximal activity, 90°C: 32.8% of maximal activity

additional information

-

O23553

freezing tolerance of recombinant plants, overview

4.45

6.5

Hordeum sp.

-

detailed isoelectric focusing analysis of pI of different isozymes from 17 Hordeum species, some with several suspecies, four pattern groups, overview

664483

4.5

-

-

chromatofocusing

4.6

4.7

-

isoelectric focusing

4.8

6

-

isoelectric focusing analysis of isozyme pI of different cultivars, overview

664674

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

bud

D0VBH4, -

shoot tip of the bud

caryopsis

P16098

mature, of Sd1 and Sd2L barley varieties

-

commercial preparation

-

-

-

-

-

-

endosperm-specific isozyme beta-amylase1, Bmy1

endosperm

-

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

-

O23553, Q9LIR6

isozyme TR-BAMY

Arabidopsis thaliana, Glycine max, Solanum tuberosum

fruit

Musa acuminata

Q3S4X4

banana beta-amylase activity is highly correlated to a decrease in starch, being primary up-regulated by de novo synthesis

-

P16098

germinated barley, of Sd1 and Sd2L barley varieties

-

-

-

O23553, Q9LIR6

isozyme TR-BAMY

-

-

-

666599, 694627, 705377

mesophyll

-

-

-

-

tissue culture

pollen

O23553, Q9LIR6

isozyme TR-BAMY

-

-, Q9FQ07

resting, localized in the cortex and the pith of rhizomes, but not in vascular tissues, pericycle, endodermis and rhizodermis

root

-

tap root

root

-

root

O23553, Q9LIR6

isozyme TR-BAMY

-

-

-

-

endosperm

-

-

germinating

-

-

Cenchrus sp., Sorghum sp.

-

the enzyme activity increases progressively during seed germination

Sorghum sp.

-

germinating, different activities during germination in the different Sorghum sp. varieties, overview

-

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

Hordeum vulgare subsp. spontaneum, Hordeum vulgare subsp. vulgare

-

distribution of thermostable alleles/isozymes in worldwide seed collections, detailed overview

O23553, Q9LIR6

isozyme TR-BAMY

Q6Z5B2, Q6Z5B7

germinating; germinating

-

-

malted and unmalted

Zea mays

-

malted

-

-

epicotyl of etiolated germinating seedlings

seedling

O23553

-

seedling

Q6Z5B2, Q6Z5B7

very low enzyme content in var. japonica; very low enzyme content in var. japonica

-

-

-

-

-

-

additional information

-

enzyme is produced throughout exponential growth and during the early-stationary phase

208617

additional information

Aspergillus terreus, Brettanomyces naardenensis, Debaryomyces sp., Emericella nidulans, Malbranchea cinnamomea, Myceliophthora sepedonium, Nakazawaea holstii, Phaffia rhodozyma, Saccharomyces cerevisiae, Saccharomyces sp., Syncephalastrum racemosum, Thermomyces lanuginosus, Trichosporon beigelii, Wickerhamomyces anomalus

-

optimal cultivation conditions, overview

additional information

-

differentiation of beta-amylase phenotypes in cultivated barley from worldwide collections, geographical distribution, overview

664674

additional information

-

tissue-ubiquitous isozyme beta-amylase2, Bmy2

additional information

-

BAM4 is preferentially expressed in vascular tissues in source and sink organs

additional information

-

beta-amylase production starts from the post-exponential phase of bacterial growth and reached a maximum level during the early-stationary phase

additional information

Arabidopsis thaliana, Glycine max, Solanum tuberosum

-

beta-amylase production starts from the post-exponential phase of bacterial growth and reached a maximum level during the early-stationary phase

-

additional information

Syncephalastrum racemosum RR96

-

optimal cultivation conditions, overview

-

chloroplast

-

stroma of mesophyll cell chloroplasts

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

-

BAM-1, BAM-2, BAM-3, BAM-4

9507

Arabidopsis thaliana, Glycine max, Solanum tuberosum

chloroplast stroma

-

-, Q9FQ07

exclusively located in

-

D0VBH4, -

BAM1 also surrounds the amyloplasts in mature cells

5829

Emericella nidulans

-

-

208601, 208608

-

-

partially cell-bound

-

-

-

208641, 677409

-

208612, 208617, 654141, 677409, 677715

-

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

-

678089

-

the enzyme is secreted

-

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

-

Bacillus megaterium DSM319, Emericella nidulans 45

-

-

the enzyme is secreted

-

Hordeum vulgare subsp. spontaneum, Hordeum vulgare subsp. vulgare

Paenibacillus polymyxa No. 26-1, Xanthophyllomyces dendrorhous CECT1690

-

germ plasm

-

cultivated, thermostable alleles/isozymes of the enzyme

60293

intracellular

-

I3ZTN9

-

-

-

-

plastid

O23553, Q9LIR6

plastid-targeted isozyme TR-BAMY, contains a plastid transit peptide of 41 amino acids

-

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

208616

56310

-

-

isoenzyme IV, electrospray ionization mass spectroscopy

57000

-

-

gel filtration

57000

-

-

equilibrium sedimentaion

208616

57200

-

-

equilibrium sedimentation

208626

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

67120

-

I3ZTN9

-

67500

-

-

BAM-1

68000

-

-

208606

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

208629

209000

-

-

variant Tainung, gel filtration

210000

-

-

gel filtration

239000

-

-

variant Chailai, gel filtration

240000

-

-

gel filtration

315000

-

-

enzyme modified with periodate-oxidized maltohexaose, gel filtration

208596

?

-

x * 61000, SDS-PAGE

?

-

x * 55000, SDS-PAGE

208600

?

-

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

208616

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

I3ZTN9

1 * 70000, SDS-PAGE

monomer

Bacillus megaterium B6

-

1 * 102000, SDS-PAGE

-

monomer

Paenibacillus polymyxa No. 26-1

-

1 * 53000, SDS-PAGE

-

pentamer

-

5 * 64000, enzyme modified with periodate-oxidized maltohexaose, SDS-PAGE

208596

tetramer

-

4 * 51000, SDS-PAGE

tetramer

-

4 * 26000, SDS-PAGE

monomer

Thermococcus sp. CL1

-

1 * 70000, 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

-

no glycoprotein

-, Q9FQ07

-

glycoprotein

Emericella nidulans

-

0.8% carbohydrate

glycoprotein

Emericella nidulans 45

-

0.8% carbohydrate

-

glycoprotein

-

intracellular enzyme contains 0.8% carbohydrate

208609

no glycoprotein

-

extracellular enzyme contains no carbohydrate moiety

208609

no glycoprotein

-

contains no carbohydrate

208600

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

208596

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

208598

additional information

-, Q9FQ07

apart from the removal of the N-terminal methionine no co- or posttranslational processing

-

-

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

-

208645

purified recombinant wild-type and mutant T47M/Y164E/T328N, hanging drop vapour diffusion method, 18°C, 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

-

208637

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, 4°C, 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, 4°C, 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

-

-

-

-

-

208646

2.5

-

-

tertiary structure is entirely disturbed

208615

3

11

-, Q9FQ07

stable in the range

3

12

-, Q9FQ07

irreversible inactivation below pH 3 and above pH 12

3.5

6.5

-

stable

3.5

7

-

70°C, in presence of 5 mM CaCl2

3.5

9

-

15 h, 20°C, 50 mM McIlvaine’s buffer and sodium carbonate-boric acid buffer, stable in the range

3.5

9.5

-

stable

3.7

-

-

stable

4

12

-

4°C, 24 h, stable

4

8

Emericella nidulans

-

50°C, 1 h, enzyme retains more than 80% of the activity

4

9

-

15 h, 37°C, stable

4.3

8.5

Dioscorea batatus

-

30°C, 60 min, stable

4.5

7.5

-

30°C, 1.5 h, stable

Hordeum vulgare, Triticum aestivum

5

6

-

immobilized enzyme, highest stability

208620

5

8.5

-

stable

5

-

-

2 months, about 80% loss of activity

6

8

-

37°C, 90 min, stable

6

8

-

30 min, stable

6.5

7.5

Emericella nidulans

-

50°C, 1 h, stable

6.5

7.5

-

90% stability between pH 6.5 and 7.5

7

11.5

-

20°C, 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

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

-

Emericella nidulans

-

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

-

Emericella nidulans

-

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

-

Hordeum sp.

-

30 min, analysis of isozyme thermostability of different species and subspecies, overview

664483

57.5

-

-

30 min, analysis of isozyme thermostability of different cultivars, overview

664674

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

-

Emericella nidulans

-

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

208620

60

-

-

rather stable at

60

-

-

in presence of 5% starch, entirely stable

60

-

-

temperature optimum, but enzyme loses activity when exposed to 60°C, 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 60°C 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

67

-

I3ZTN9

melting temperature at pH 4.0

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

-

-

60 min, stable

70

-

-

pH 4.8, half-life: 14.4 min for the first decay segment, 37.9 min for the second decay segment

208620

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

85

-

I3ZTN9

the half-life is 69 min, 225 min, and 255 min at pH 5.0, pH 6.0, and pH 7.0

91

-

I3ZTN9

melting temperature at pH 5.0

105

-

I3ZTN9

melting temperature at pH 6.0

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 1.9°C and 2.1°C, 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 enzyme’s environment by the addition of Mn2+ and 2-mercaptoethanol, and through immobilization. Both of which would increase the enzyme’s practical importance and industrial utility

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

-

208615

SDS, effective in disturbing the tertiary structure, no effect on secondary structure

-

208615

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

-

Ethanol

-

10% v/v, 1 h, 65°C, completely stable

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

the activity in roots at 4-16°C during storage is immediately increased after beginning

-

4°C, stable for 3 weeks

-

3°C, in presence of 0.05 M beta-mercaptoethanol, 50% loss of activity after 1 week

-

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

4100fold

-

-

-, Q9FQ07

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

-

-

-

208641, 208646

beta-amylase I and II

-

-

-

-

-

partial

-

-

-

-

-

-

-

208601, 208608, 680294

partial

-

-

-

partially by preparation of enzyme extract and heat treatment at 70°C 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

Zea mays

-

681063

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

-

208598

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

-

-, Q9FQ07

-

-

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

Musa acuminata

Q3S4X4

682492

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

-

-

208606

-

-

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

-

680294

expressed the gene in Escherichia coli

I3ZTN9

cold-stress treatment, 4°C for 24 h

Camellia sinensis

-

700766

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

-

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 60°C compared to the wild-type enzyme

G48A/A51E

-, P06547

site-directed mutagenesis, the mutant shows increased thermostability at 60°C compared to the wild-type enzyme

I74V

-, P06547

site-directed mutagenesis, the mutant shows similar thermostability at 60°C as the wild-type enzyme

L135V

-, P06547

site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme

L172F/Y173L

-, P06547

site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme

R118Q

-, P06547

site-directed mutagenesis, the mutant shows increased thermostability at 60°C compared to the wild-type enzyme

R311P/I312L

-, P06547

site-directed mutagenesis, the mutant shows similar thermostability at 60°C as the wild-type enzyme

R311P/I312L/S317A

-, P06547

site-directed mutagenesis, the mutant shows increased thermostability at 60°C 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 60°C 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 60°C compared to the wild-type enzyme

T116M/R118Q

-, P06547

site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme

T76V

-, P06547

site-directed mutagenesis, the mutant shows similar thermostability at 60°C as the wild-type enzyme

T98K/Y99L/A100V/D101E

-, P06547

site-directed mutagenesis, the mutant shows increased thermostability at 60°C compared to the wild-type enzyme

Y72D

-, P06547

site-directed mutagenesis, the mutant shows similar thermostability at 60°C as the wild-type enzyme

Y72D/I74V/T76V

-, P06547

site-directed mutagenesis, the mutant shows increased thermostability at 60°C 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 60°C compared to the wild-type enzyme

-

T76V

Bacillus circulans NCIMB 11033

-

site-directed mutagenesis, the mutant shows similar thermostability at 60°C 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 2.1°C 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 1.9°C, 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 4°C

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 25°C 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 60°C 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 60°C 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

680294

No entries in this field

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 75°C

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