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Information on EC 3.2.1.1 - alpha-amylase and Organism(s) Pseudoalteromonas haloplanktis and UniProt Accession P29957

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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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Pseudoalteromonas haloplanktis
UNIPROT: P29957
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Word Map
The taxonomic range for the selected organisms is: Pseudoalteromonas haloplanktis
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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-
-
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Alpha-amylase carcinoid
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-
-
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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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-
-
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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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-
-
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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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-
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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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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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Ptyalin
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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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Thermolase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units
show the reaction diagram
active site mobility and structure of the psychrophilic alpha-amylase, ligand binding mechanism and conformational changes, side chains involved in substrate binding are strictly conserved, overview
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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
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene + H2O
4-nitrophenol + 4,6-O-ethylidene-[G7]-alpha-D-maltoheptaose
show the reaction diagram
-
-
-
?
2 starch + H2O
2 malto-oligosaccharides + maltose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene + H2O
4-nitrophenol + 4,6-O-ethylidene-[G7]-alpha-D-maltoheptaose
show the reaction diagram
-
-
-
-
?
starch + H2O
maltooligosaccharides
show the reaction diagram
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-
-
-
?
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
2 starch + H2O
2 malto-oligosaccharides + maltose
show the reaction diagram
-
-
-
-
?
starch + H2O
maltooligosaccharides
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
chloride
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is a weak allosteric enzyme activator
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
maltose
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product inhibition, the active site able to accomodate larger inhibitory complxes, resulting in a mixed type inhibition of starch hydrolysis
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.223
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
pH not specified in the publication, 25°C
0.23
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
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25°C, pH 7.2
additional information
additional information
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isothermal titration and microcalorimetric analysis, thermodynamics and kinetics
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
675
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
pH not specified in the publication, 25°C
179
starch
pH not specified in the publication, 5°C
392 - 697
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3000
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
pH not specified in the publication, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
inhibition kinetics
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
cold-active, psychrophilic alpha-amylase
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
comparison of chloride-dependent alpha-amylases from a psychrophilic Antarctic bacterium, the ectothermic fruit fly, the homeothermic pig and from a thermophilic actinomycete reveals striking continuum in the functional properties of the enzymes coupled to their structural stability and related to the thermal regime of the source organism
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AMY_PSEHA
669
0
73268
Swiss-Prot
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K300R
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47% of wild-type kcat
K300R/N150D/V196F/Q164I/T232V
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44% of wild-type kcat, increase in temperature stability
N150D
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98% of wild-type kcat
Q164I
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73% of wild-type kcat
T232V
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105% of wild-type kcat
V196F
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108% of wild-type kcat
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44.1
melting temperature
45
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wild-type, approx. 70% loss of activity after 45 min in the absence of starch, approx. 95% loss of activity after 45 min in the presence of 2% starch, K300R/N150D/V196F/Q164I/T232V mutant, approx. 50% loss of activity in the absence of starch
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of AHA mutants in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
D'Amico, S.; Gerday, C.; Feller, G.
Temperature adaptation of proteins: engineering mesophilic-like activity and stability in a cold-adapted alpha-amylase
J. Mol. Biol.
332
981-988
2003
Pseudoalteromonas haloplanktis, Sus scrofa
Manually annotated by BRENDA team
D'Amico, S.; Sohier, J.S.; Feller, G.
Kinetics and energetics of ligand binding determined by microcalorimetry: insights into active site mobility in a psychrophilic alpha-amylase
J. Mol. Biol.
358
1296-1304
2006
Pseudoalteromonas haloplanktis
Manually annotated by BRENDA team
Cipolla, A.; Delbrassine, F.; Da Lage, J.L.; Feller, G.
Temperature adaptations in psychrophilic, mesophilic and thermophilic chloride-dependent alpha-amylases
Biochimie
94
1943-1950
2012
Sus scrofa (P00690), Drosophila melanogaster (P08144), Pseudoalteromonas haloplanktis (P29957), Thermobifida fusca (Q47R94)
Manually annotated by BRENDA team