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

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Oryza sativa
UNIPROT: P17654
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea


The taxonomic range for the selected organisms is: Oryza sativa

EC NUMBER
COMMENTARY hide
3.2.1.1
-
RECOMMENDED NAME
GeneOntology No.
alpha-amylase
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
starch degradation
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Starch and sucrose metabolism
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Metabolic pathways
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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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isozyme AmyI-1; cultivar Nipponbare
UniProt
Manually annotated by BRENDA team
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
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
P17654
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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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
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isoenzyme Amy1A
5
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isoenzyme Amy3D
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PDB
SCOP
CATH
UNIPROT
ORGANISM
-
-
-
-
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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glycoprotein
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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
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the intracellular enzyme contains no carbohydrate
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
1 h, with 25% w/v raw corn starch, 24% loss of activity
26
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1 h, with 25% w/v raw corn starch, 11% loss of activity
37
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1 h, with 25% w/v raw corn starch, 3% loss of activity
78
-
5 min, chimeric enzyme, about 90% loss of activity
additional information
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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
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Saccharomyces cerevisiae
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N240Q
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mutant of isoenzyme Amy1A
additional information