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Information on EC 3.2.1.204 - 1,3-alpha-isomaltosidase and Organism(s) Kribbella flavida and UniProt Accession D2PPM7

for references in articles please use BRENDA:EC3.2.1.204
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IUBMB Comments
The enzyme, characterized from the bacteria Bacillus sp. NRRL B-21195 and Kribbella flavida, participates in the degradation of starch. The cyclic tetrasaccharide cyclobis-(1->6)-alpha-nigerosyl is formed from starch extracellularly and imported into the cell, where it is degraded to glucose.
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This record set is specific for:
Kribbella flavida
UNIPROT: D2PPM7
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The taxonomic range for the selected organisms is: Kribbella flavida
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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Synonyms
kfla1895, cycloalternan isomaltosylhydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
1,3-alpha-isomaltohydrolase (configuration-retaining)
The enzyme, characterized from the bacteria Bacillus sp. NRRL B-21195 and Kribbella flavida, participates in the degradation of starch. The cyclic tetrasaccharide cyclobis-(1->6)-alpha-nigerosyl is formed from starch extracellularly and imported into the cell, where it is degraded to glucose.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
cyclobis-(1->6)-alpha-nigerosyl + 2 H2O
2 isomaltose
show the reaction diagram
-
-
-
?
panose + H2O
isomaltose + alpha-D-glucopyranose
show the reaction diagram
-
-
-
?
additional information
?
-
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
cyclobis-(1->6)-alpha-nigerosyl + 2 H2O
2 isomaltose
show the reaction diagram
-
-
-
?
additional information
?
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.63
cyclobis-(1->6)-alpha-nigerosyl
pH 8.0, 35°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
22.3
cyclobis-(1->6)-alpha-nigerosyl
pH 8.0, 35°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.052
panose
pH 8.0, 35°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
glycoside hydrolase family 31 protein
UniProt
Manually annotated by BRENDA team
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 10.7
-
742891
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41
stable below
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tagami, T.; Miyano, E.; Sadahiro, J.; Okuyama, M.; Iwasaki, T.; Kimura, A.
Two novel glycoside hydrolases responsible for the catabolism of cyclobis-(1->6)-alpha-nigerosyl
J. Biol. Chem.
291
16438-16447
2016
Kribbella flavida (D2PPM7), Kribbella flavida, Kribbella flavida DSM 17836 (D2PPM7)
Manually annotated by BRENDA team