KEGG   ENZYME: 3.2.1.214
Entry
EC 3.2.1.214                Enzyme                                 
Name
exo beta-1,2-glucooligosaccharide sophorohydrolase (non-reducing end)
Class
Hydrolases;
Glycosylases;
Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
Sysname
exo (1->2)-beta-D-glucooligosaccharide sophorohydrolase (non-reducing end)
Reaction(IUBMB)
[(1->2)-beta-D-glucosyl]n + H2O = sophorose + [(1->2)-beta-D-glucosyl]n-2 [RN:R12634]
Reaction(KEGG)
R12634
Substrate
[(1->2)-beta-D-glucosyl]n [CPD:C02490];
H2O [CPD:C00001]
Product
sophorose [CPD:C08250];
[(1->2)-beta-D-glucosyl]n-2 [CPD:C02490]
Comment
The enzyme, characterized from the bacterium Parabacteroides distasonis, specifically hydrolyses (1->2)-beta-D-glucooligosaccharides to sophorose. The best substrates are the tetra- and pentasaccharides. The enzyme is not able to cleave the trisaccharide, and activity with longer linear (1->2)-beta-D-glucans is quite low. This enzyme acts in exo mode and is not able to hydrolyse cyclic (1->2)-beta-D-glucans.
History
EC 3.2.1.214 created 2020
Orthology
K24289  exo beta-1,2-glucooligosaccharide sophorohydrolase (non-reducing end)
Genes
BGOK: Pr1d_27430
PDI: BDI_3064
PARC: CI960_21510
GFL: GRFL_2144
AFLA: FHG64_05370
CTUR: LNP04_19240
EZE: KI430_07445
Reference
1  [PMID:29763309]
  Authors
Shimizu H, Nakajima M, Miyanaga A, Takahashi Y, Tanaka N, Kobayashi K, Sugimoto N, Nakai H, Taguchi H
  Title
Characterization and Structural Analysis of a Novel exo-Type Enzyme Acting on beta-1,2-Glucooligosaccharides from Parabacteroides distasonis.
  Journal
Biochemistry 57:3849-3860 (2018)
DOI:10.1021/acs.biochem.8b00385
  Sequence
[pdi:BDI_3064]
Other DBs
ExplorEnz - The Enzyme Database: 3.2.1.214
IUBMB Enzyme Nomenclature: 3.2.1.214
ExPASy - ENZYME nomenclature database: 3.2.1.214
BRENDA, the Enzyme Database: 3.2.1.214

  All links  
Chemical substance (3)   
   KEGG COMPOUND (3)   
Chemical reaction (1)   
   KEGG REACTION (1)   
Gene (8)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (7)   
Protein sequence (2)   
   UniProt (1)   
   SWISS-PROT (1)   
Protein domain (2)   
   InterPro (2)   
All databases (16)   

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