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Information on EC 3.2.1.1 - alpha-amylase and Organism(s) Oryza sativa and UniProt Accession P17654

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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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Oryza sativa
UNIPROT: P17654
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The taxonomic range for the selected organisms is: Oryza sativa
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
AmyI-1
isozyme
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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amylase, alpha-
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-
-
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Amylopsin
-
-
-
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Bactosol TK
-
-
-
-
Buclamase
-
-
-
-
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
-
-
-
-
G 995
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-
-
-
glycogenase
-
-
-
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High pI alpha-amylase
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-
-
-
Isozyme 1B
-
-
-
-
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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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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-
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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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
starch + H2O
malto-oligosaccharides
show the reaction diagram
-
-
-
?
maltoheptaose + H2O
additional information
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
starch + H2O
malto-oligosaccharides
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
95% loss of activity after removal of Ca2+ by EDTA, addition of Ca2+ results in the recovery of 12% of the original activity, alpha-amylase III
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 4.5
-
isoenzyme Amy1A
5
-
isoenzyme Amy3D
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isozyme AmyI-1; cultivar Nipponbare
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Golgi-to-plastid traffic appears to be involved in the transport of glycoproteins to plastids
Manually annotated by BRENDA team
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
glycoprotein
-
isoenzyme Amy1A has an N-linked carbohydrate chain in the mature protein, isoenzyme Amy3D and chimeric enzyme Amy1A/3D do not contain N-linked carbohydrate chain
no modification
-
the intracellular enzyme contains no carbohydrate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N240Q
-
mutant of isoenzyme Amy1A
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26
-
1 h, with 25% w/v raw corn starch, 11% loss of activity
37
-
1 h, with 25% w/v raw corn starch, 3% loss of activity
4
-
1 h, with 25% w/v raw corn starch, 24% loss of activity
78
-
5 min, chimeric enzyme, about 90% loss of activity
additional information
-
isoenzyme Amy1A shows the highest thermostability, mutant enzyme N240Q of isoenzyme Amy1A shows almost identical thermostability to those of Amy3D and Amy1A/3D
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
alpha-amylase III
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Saccharomyces cerevisiae
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chiba, Y.; Nieda, Y.; Nakayima, T.; Ichishima, E.
Unique enzymatic properties of alpha-amylase-III from suspension-cultured rice cells
Agric. Biol. Chem.
55
901-902
1991
Oryza sativa
Manually annotated by BRENDA team
Terashima, M.; Kawai, M.; Kumagai, M.H.; Rodriguez, R.L.; Katoh, S.
Characteristics of a chimeric enzyme engineered from two rice alpha-amylase isozymes
Appl. Microbiol. Biotechnol.
45
607-611
1996
Oryza sativa
-
Manually annotated by BRENDA team
Terashima, M.; Katoh, S.
Modification of alpha-amylase functions by protein engineering
Ann. N. Y. Acad. Sci.
799
65-69
1996
Oryza sativa
Manually annotated by BRENDA team
Kitajima, A.; Asatsuma, S.; Okada, H.; Hamada, Y.; Kaneko, K.; Nanjo, Y.; Kawagoe, Y.; Toyooka, K.; Matsuoka, K.; Takeuchi, M.; Nakano, A.; Mitsui, T.
The rice alpha-amylase glycoprotein is targeted from the Golgi apparatus through the secretory pathway to the plastids
Plant Cell
21
2844-2858
2009
Oryza sativa (P17654), Oryza sativa
Manually annotated by BRENDA team