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Information on EC 3.2.1.2 - beta-amylase and Organism(s) Niallia circulans and UniProt Accession P06547

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EC Tree
     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.2 beta-amylase
IUBMB Comments
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.
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This record set is specific for:
Niallia circulans
UNIPROT: P06547
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Word Map
The taxonomic range for the selected organisms is: Niallia circulans
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
beta-amylase, arath, spoii, beta amylase, tr-bamy, ct-bmy, bam-2, beta-amylase 1, glycogenase, bam-8, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(1-4)-alpha-D-glucan maltohydrolase
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1,4-alpha-D-glucan maltohydrolase
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amylase, beta-
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beta amylase
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glycogenase
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saccharogen amylase
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saccharogenamylase
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SYSTEMATIC NAME
IUBMB Comments
4-alpha-D-glucan maltohydrolase
Acts on starch, glycogen and related polysaccharides and oligosaccharides producing beta-maltose by an inversion. The term 'beta'' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolysed.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-91-3
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
beta-amylase-inhibitor
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several strains of Streptomyces produce a beta-amylase inhibitor when grown on a medium containing starch and deoxynojirimycin
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AMYB_NIACI
575
1
62899
Swiss-Prot
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
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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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D170Q/L172F/Y173L
site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme
G48A/A51E
site-directed mutagenesis, the mutant shows increased thermostability at 60°C compared to the wild-type enzyme
I74V
site-directed mutagenesis, the mutant shows similar thermostability at 60°C as the wild-type enzyme
L135V
site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme
L172F/Y173L
site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme
L172F/Y173L/A174E
site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme
R118Q
site-directed mutagenesis, the mutant shows increased thermostability at 60°C compared to the wild-type enzyme
R311P/I312L
site-directed mutagenesis, the mutant shows similar thermostability at 60°C as the wild-type enzyme
R311P/I312L/S317A
site-directed mutagenesis, the mutant shows increased thermostability at 60°C compared to the wild-type enzyme
S133N/L135V
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
S137T/K138A
site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme
S317A
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
T116M
site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme
T116M/R118Q
site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme
T76V
site-directed mutagenesis, the mutant shows similar thermostability at 60°C as the wild-type enzyme
T98K/Y99L/A100V/D101E
site-directed mutagenesis, the mutant shows increased thermostability at 60°C compared to the wild-type enzyme
Y72D
site-directed mutagenesis, the mutant shows similar thermostability at 60°C as the wild-type enzyme
Y72D/I74V/T76V
site-directed mutagenesis, the mutant shows increased thermostability at 60°C compared to the wild-type enzyme
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
half-life of the wild-type enzyme is 6.4 min
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
phylogenetic analysis, expression of wild-type and mutant enzymes in Escherichia coli Rosetta2 cells, subcloning in strain JM109
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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Siggens, K.W.
Molecular cloning and characterization of the beta-amylase gene from Bacillus circulans
Mol. Microbiol.
1
86-91
1987
Niallia circulans
Manually annotated by BRENDA team
Arai, M.; Sumida, M.; Nakatani, S.; Murao, S.
A novel beta-amylase inhibitor
Agric. Biol. Chem.
47
183-185
1983
Niallia circulans, Priestia megaterium, Glycine max, Hordeum vulgare, Ipomoea batatas
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Manually annotated by BRENDA team
Yamashiro, K.; Yokobori, S.; Koikeda, S.; Yamagishi, A.
Improvement of Bacillus circulans beta-amylase activity attained using the ancestral mutation method
Protein Eng. Des. Sel.
23
519-528
2010
Niallia circulans (P06547), Niallia circulans, Niallia circulans NCIMB 11033 (P06547)
Manually annotated by BRENDA team