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EC Tree
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.
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,
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1,4-alpha-D-glucan glucanohydrolase
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Alpha-amylase carcinoid
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Clones GRAMY56 and 963
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High pI alpha-amylase
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Low pI alpha-amylase
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Meiotic expression upregulated protein 30
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Pancreatic alpha-amylase
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Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units
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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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.
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4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene + H2O
4-nitrophenol + 4,6-O-ethylidene-[G7]-alpha-D-maltoheptaose
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2 starch + H2O
2 malto-oligosaccharides + maltose
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4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene + H2O
4-nitrophenol + 4,6-O-ethylidene-[G7]-alpha-D-maltoheptaose
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starch + H2O
maltooligosaccharides
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2 starch + H2O
2 malto-oligosaccharides + maltose
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starch + H2O
maltooligosaccharides
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chloride
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is a weak allosteric enzyme activator
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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
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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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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
392
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
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15°C, pH 7.2
697
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
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25°C, pH 7.2
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3000
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
pH not specified in the publication, 25°C
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additional information
additional information
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inhibition kinetics
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additional information
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cold-active, psychrophilic alpha-amylase
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UniProt
brenda
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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
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AMY_PSEHA
669
0
73268
Swiss-Prot
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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
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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
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expression of AHA mutants in Escherichia coli
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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
brenda
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
brenda
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)
brenda
Transporter Classification Database (TCDB):
8.A.9.1.3