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Information on EC 3.2.1.1 - alpha-amylase and Organism(s) Saccharolobus solfataricus and UniProt Accession D0KTV8

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IUBMB Comments
Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. The term "alpha" 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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Saccharolobus solfataricus
UNIPROT: D0KTV8
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The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The enzyme appears in selected viruses and cellular organisms
Synonyms
alpha-amylase, diastase, alpha amylase, pancreatic alpha-amylase, crustacean cardioactive peptide, maltogenic amylase, taka-amylase a, human salivary alpha-amylase, bacillus licheniformis alpha-amylase, alpha-amylase 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,4-alpha-D-glucan glucanohydrolase
-
-
-
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Alpha-amylase carcinoid
-
-
-
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Amy c6
-
-
-
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AMY1
-
-
-
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Amylase THC 250
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-
-
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amylase, alpha-
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-
-
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Amylopsin
-
-
-
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Bactosol TK
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-
-
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Buclamase
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-
-
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Clarase
-
-
-
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Clone 103
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-
-
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Clone 168
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-
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Clone PHV19
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-
-
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Clones GRAMY56 and 963
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-
-
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diastase
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-
-
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endoamylase
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-
-
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Fortizyme
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-
-
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G 995
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-
-
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glycogenase
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-
-
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High pI alpha-amylase
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-
-
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Isozyme 1B
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-
-
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Kleistase L 1
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-
-
-
Low pI alpha-amylase
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-
-
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Maxamyl
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-
-
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Maxilase
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-
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Meiotic expression upregulated protein 30
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-
-
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Pancreatic alpha-amylase
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-
-
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Pivozin
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-
-
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Ptyalin
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-
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Spitase CP 1
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-
-
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TAA
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-
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Taka-amylase A
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-
-
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Takatherm
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-
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Thermamyl
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Thermolase
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-
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SYSTEMATIC NAME
IUBMB Comments
4-alpha-D-glucan glucanohydrolase
Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. The term "alpha" 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
9000-90-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-cyclodextrin + H2O
?
show the reaction diagram
-
catalyzes the hydrolysis of starch, dextrin, and alpha-cyclodextrin with similar efficiencies
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-
?
dextrin + H2O
maltooligosaccharides
show the reaction diagram
-
catalyzes the hydrolysis of starch, dextrin, and alpha-cyclodextrin with similar efficiencies
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-
?
starch + H2O
?
show the reaction diagram
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catalyzes the hydrolysis of starch, dextrin, and alpha-cyclodextrin with similar efficiencies
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-
?
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.05
calculated from sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the alpha-amylase is essential for growth on starch, glycogen, and pullulan
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120000
-
2 * 120000, SDS-PAGE
240000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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2 * 120000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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high level production in high-cell density culture of the food yeast Candida utilis. Expression of this synthetic gene under the control of the GAP promoter yields biologically active alpha-mylase, accounting for more than 50% of the soluble protein
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
glycosyl hydrolase production in Sulfolobus solfataricus requires a trans-acting factor for wild-type levels of expression
aspartate is identified as the most repressing sole carbon source for alpha-amylase production. Repression by glucose
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constitutively produced at low levels but can be induced further by starch addition
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glutamate is the most derepressing sole carbon source for alpha-amylase production
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induction when cells which were maintained in sucrose minimal medium with yeast extract are down shifted to sucrose minimal medium without yeast extract addtion
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levels of alpha-amylase mRNA are reduced 10fold as a consequence of yeast extract medium supplementation to sucrose minimal medium
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Haseltine, C.; Montalvo-Rodriguez, R.; Carl, A.; Bini, E.; Blum, P.
Extragenic pleiotropic mutations that repress glycosyl hydrolase expression in the hyperthermophilic archaeon Sulfolobus solfataricus
Genetics
152
1353-1361
1999
Saccharolobus solfataricus (D0KTV8), Saccharolobus solfataricus, Saccharolobus solfataricus 98/2 (D0KTV8)
Manually annotated by BRENDA team
Kobayashi, K.; Komeda, T.; Miura, Y.; Kettoku, M.; Kato, M.
Production of trehalose from starch by novel trehalose-producing enzymes from Sulfolobus solfataricus KM1
J. Ferment. Bioeng.
83
296-298
1997
Saccharolobus solfataricus, Saccharolobus solfataricus KM1
-
Manually annotated by BRENDA team
Haseltine, C.; Rolfsmeier, M.; Blum, P.
The glucose effect and regulation of alpha-amylase synthesis in the hyperthermophilic archaeon Sulfolobus solfataricus
J. Bacteriol.
178
945-950
1996
Saccharolobus solfataricus, Saccharolobus solfataricus 2
Manually annotated by BRENDA team
Haseltine, C.; Montalvo-Rodriguez, R.; Bini, E.; Carl, A.; Blum, P.
Coordinate transcriptional control in the hyperthermophilic archaeon Sulfolobus solfataricus
J. Bacteriol.
181
3920-3927
1999
Saccharolobus solfataricus
Manually annotated by BRENDA team
Worthington, P.; Hoang, V.; Perez-Pomares, F.; Blum, P.
Targeted disruption of the alpha-amylase gene in the hyperthermophilic archaeon Sulfolobus solfataricus
J. Bacteriol.
185
482-488
2003
Saccharolobus solfataricus (Q97YY0), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97YY0)
Manually annotated by BRENDA team
Miura, Y.; Kettoku, M.; Kato, M.; Kobayashi, K.; Kondo, K.
High level production of thermostable alpha-amylase from Sulfolobus solfataricus in high-cell density culture of the food yeast Candida utilis
J. Mol. Microbiol. Biotechnol.
1
129-134
1999
Saccharolobus solfataricus
Manually annotated by BRENDA team