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Information on EC 3.2.1.1 - alpha-amylase and Organism(s) Thermobifida fusca and UniProt Accession Q1KLC8

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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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Thermobifida fusca
UNIPROT: Q1KLC8
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The taxonomic range for the selected organisms is: Thermobifida fusca
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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-
-
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Amy c6
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-
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AMY1
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-
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Amylase THC 250
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-
-
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amylase, alpha-
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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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Clone 103
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Clone 168
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Clone PHV19
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Clones GRAMY56 and 963
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-
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diastase
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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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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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Meiotic expression upregulated protein 30
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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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TAA
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Taka-amylase A
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Takatherm
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Thermamyl
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Thermolase
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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
raw sago starch + H2O
?
show the reaction diagram
high level of activity
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-
?
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
?
show the reaction diagram
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.26
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
pH not specified in the publication, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
153
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
pH not specified in the publication, 25°C
1457
starch
pH not specified in the publication, 55°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
600
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
pH not specified in the publication, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
61.65
purified recombinant enzyme, pH 7.0, 60°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from compost soils collected in Taiwan
UniProt
Manually annotated by BRENDA team
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?
Q1KLC8_THEFU
605
1
64678
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65000
x * 65000, recombinant enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 65000, recombinant enzyme, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
purified recombinant enzyme, 4°C, 24 h, stable
717948
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
74
melting temperature
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant extracellular enzyme expressed from Yarrowia lipolytica strain P01g 10.8fold by ultrafiltration, anion exchange chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
high level recombinant expression in Pichia pastoris X-33 host strain using vector pGAPZaA, allowing constitutive expression and secretion of the protein
high level recombinant expression in Yarrowia lipolytica strain P01g using the vector pYLSC1 allowing constitutive expression and secretion of the protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yang, C.; Huang, Y.; Chen, C.; Wen, C.
Expression of Thermobifida fusca thermostable raw starch digesting alpha-amylase in Pichia pastoris and its application in raw sago starch hydrolysis
J. Ind. Microbiol. Biotechnol.
37
401-406
2010
Thermobifida fusca (Q1KLC8), Thermobifida fusca, Thermobifida fusca NTU22 (Q1KLC8), Thermobifida fusca NTU22
Manually annotated by BRENDA team
Yang, C.H.; Huang, Y.C.; Chen, C.Y.; Wen, C.Y.
Heterologous expression of Thermobifida fusca thermostable alpha-amylase in Yarrowia lipolytica and its application in boiling stable resistant sago starch preparation
J. Ind. Microbiol. Biotechnol.
37
953-960
2010
Thermobifida fusca (Q1KLC8), Thermobifida fusca NTU22 (Q1KLC8)
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