KEGG   ENZYME: 3.2.1.204Help
Entry
EC 3.2.1.204                Enzyme                                 

Name
1,3-alpha-isomaltosidase
Class
Hydrolases;
Glycosylases;
Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
BRITE hierarchy
Sysname
1,3-alpha-isomaltohydrolase (configuration-retaining)
Reaction(IUBMB)
cyclobis-(1->6)-alpha-nigerosyl + 2 H2O = 2 isomaltose (overall reaction) [RN:R11788];
(1a) cyclobis-(1->6)-alpha-nigerosyl + H2O = alpha-isomaltosyl-(1->3)-isomaltose [RN:R11789];
(1b) alpha-isomaltosyl-(1->3)-isomaltose + H2O = 2 isomaltose [RN:R11790]
Reaction(KEGG)
Substrate
cyclobis-(1->6)-alpha-nigerosyl;
H2O [CPD:C00001];
alpha-isomaltosyl-(1->3)-isomaltose
Product
isomaltose [CPD:C00252];
alpha-isomaltosyl-(1->3)-isomaltose
Comment
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.
History
EC 3.2.1.204 created 2017
Orthology
K22307  1,3-alpha-isomaltosidase
Genes
NCA: Noca_4630
KFL: Kfla_1895
NOA: BKM31_21905
TPY: CQ11_05330
TPYO: X956_02375
AYM: YM304_31640
Taxonomy
Reference
1  [PMID:15063208]
  Authors
Kim YK, Kitaoka M, Hayashi K, Kim CH, Cote GL
  Title
Purification and characterization of an intracellular cycloalternan-degrading enzyme from Bacillus sp. NRRL B-21195.
  Journal
Carbohydr Res 339:1179-84 (2004)
DOI:10.1016/j.carres.2004.02.008
Reference
2  [PMID:27302067]
  Authors
Tagami T, Miyano E, Sadahiro J, Okuyama M, Iwasaki T, Kimura A
  Title
Two Novel Glycoside Hydrolases Responsible for the Catabolism of Cyclobis-(1-->6)-alpha-nigerosyl.
  Journal
J Biol Chem 291:16438-47 (2016)
DOI:10.1074/jbc.M116.727305
  Sequence
[kfl:Kfla_1895]
Other DBs
ExplorEnz - The Enzyme Database: 3.2.1.204
IUBMB Enzyme Nomenclature: 3.2.1.204
ExPASy - ENZYME nomenclature database: 3.2.1.204
BRENDA, the Enzyme Database: 3.2.1.204

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