Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.2.1.1 - alpha-amylase and Organism(s) Bacteroides thetaiotaomicron and UniProt Accession Q8A1G3

for references in articles please use BRENDA:EC3.2.1.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Bacteroides thetaiotaomicron
UNIPROT: Q8A1G3
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Bacteroides thetaiotaomicron
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
-
-
-
-
Alpha-amylase carcinoid
-
-
-
-
Amy c6
-
-
-
-
AMY1
-
-
-
-
Amylase THC 250
-
-
-
-
amylase, alpha-
-
-
-
-
Amylopsin
-
-
-
-
Bactosol TK
-
-
-
-
Buclamase
-
-
-
-
Clarase
-
-
-
-
Clone 103
-
-
-
-
Clone 168
-
-
-
-
Clone PHV19
-
-
-
-
Clones GRAMY56 and 963
-
-
-
-
diastase
-
-
-
-
endoamylase
-
-
-
-
Fortizyme
-
-
-
-
G 995
-
-
-
-
glycogenase
-
-
-
-
High pI alpha-amylase
-
-
-
-
Isozyme 1B
-
-
-
-
Kleistase L 1
-
-
-
-
Low pI alpha-amylase
-
-
-
-
Maxamyl
-
-
-
-
Maxilase
-
-
-
-
Meiotic expression upregulated protein 30
-
-
-
-
Pancreatic alpha-amylase
-
-
-
-
Pivozin
-
-
-
-
Ptyalin
-
-
-
-
Spitase CP 1
-
-
-
-
TAA
-
-
-
-
Taka-amylase A
-
-
-
-
Takatherm
-
-
-
-
Thermamyl
-
-
-
-
Thermolase
-
-
-
-
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
amylopectin + H2O
?
show the reaction diagram
-
-
-
?
amylose + H2O
?
show the reaction diagram
-
-
-
?
pullulan + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
maltooligosaccharide bind to the carbohydrate-binding domain, CBM58, of SusG. SusG is flexible in its carbohydrate selectivity because it binds to and degrades pullulan, amylopectin, and amylose. It shows low activity on alpha- and beta-cyclodextrins
-
-
?
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
amylopectin + H2O
?
show the reaction diagram
-
-
-
?
amylose + H2O
?
show the reaction diagram
-
-
-
?
pullulan + H2O
?
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
2 ions per enzyme molecule
Mg2+
2 ions per enzyme molecule
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acarbose
a pseudotetrasaccharide inhibitor of alpha-amylase and alpha-glucosidase, binding structure, overview
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
human gut symbiont
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SusG is the alpha-amylase expressed concomitantly with Sus-CDEF on the outer surface of the cell and is absolutely required for growth on starch
additional information
determination of the structure of carbohydrate binding CBM58-binding site, the active site, and the surface starch-binding site, directly adjacent to the reducing end of the active site
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
SusG is composed of A, B, and C domains that share structural features with other amylases. The A domain, residues 43-152 and 364-607, has an eight-stranded alpha/beta barrel that contains the catalytic site, with the B domain, residues 153-215 and 336-363, inserted between beta3 and alpha3 of the A domain. The B domain consists of two two-stranded antiparallel beta sheets, two alpha helices, and three 310 helices that pack against the A domain and contribute to the size and accessibility of the active site. The C domain, residues 608-692, folds into an eight-stranded beta sandwich, structure model, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
SusG D498N mutant with bound maltoheptaose, Ca2+ replaces the Mg2+ ion observed in the apo structure, X-ray diffraction structure determination and analysis at 2.3 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D498N
site-directed mutagenesis, a catalytically inactive mutant, crystal structure determination and analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Koropatkin, N.M.; Smith, T.J.
SusG: a unique cell-membrane-associated alpha-amylase from a prominent human gut symbiont targets complex starch molecules
Structure
18
200-215
2010
Bacteroides thetaiotaomicron (Q8A1G3)
Manually annotated by BRENDA team