KEGG   ENZYME: 3.2.1.10Help
Entry
EC 3.2.1.10                 Enzyme                                 

Name oligo-1,6-glucosidase;
limit dextrinase (erroneous);
isomaltase;
sucrase-isomaltase;
exo-oligo-1,6-glucosidase;
dextrin 6alpha-glucanohydrolase;
alpha-limit dextrinase;
dextrin 6-glucanohydrolase;
oligosaccharide alpha-1,6-glucohydrolase
Class Hydrolases;
Glycosylases;
Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
compounds
BRITE hierarchy
Sysname oligosaccharide 6-alpha-glucohydrolase
Reaction(IUBMB) Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some
oligosaccharides produced from starch and glycogen by EC 3.2.1.1
(alpha-amylase), and in isomaltose
Reaction(KEGG) (other) R01718 R01791 R06080(G) R06199(G)
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Comment This enzyme, like EC 3.2.1.33 (amylo-alpha-1,6-glucosidase), can
release an alpha-1->6-linked glucose, whereas the shortest chain
that can be released by EC 3.2.1.41 (pullulanase), EC 3.2.1.142
(limit dextrinase), and EC 3.2.1.68 (isoamylase) is maltose. It also
hydrolyses isomaltulose (palatinose), isomaltotriose and panose, but
has no action on glycogen or phosphorylase limit dextrin. The enzyme
from intestinal mucosa is a single polypeptide chain that also
catalyses the reaction of EC 3.2.1.48 (sucrose alpha-glucosidase).
Differs from EC 3.2.1.33 (amylo-alpha-1,6-glucosidase) in its
preference for short-chain substrates and in its not requiring the
6-glucosylated residue to be at a branch point, i.e. linked at both
C-1 and C-4.
Pathway PATH: ec00500  Starch and sucrose metabolism
PATH: ec01100  Metabolic pathways
Orthology KO: K01182  oligo-1,6-glucosidase
KO: K01203  sucrase-isomaltase / oligo-1,6-glucosidase
Genes HSA: 6476(SI)
PTR: 470988(SI)
MMU: 69983(Sis)
RNO: 497756(Si)
CFA: 488141(SI)
BTA: 504366(SI)
ECB: 100063242
MDO: 100013945
EHI: EHI_130690
VVU: VV2_0256
VVY: VVA0760
PPR: PBPRB0410
PIN: Ping_2383 Ping_2908
NMU: Nmul_A1251
RET: RHE_CH03282(malL)
BSU: BSU02840(ycdG) BSU34560(malL)
BHA: BH2903
BAN: BA4231(malL)
BAR: GBAA4231(malL)
BAA: BA_4692
BAT: BAS3924
BAH: BAMEG_4272(malL)
BAI: BAA_4254(malL)
BCE: BC4015
BCA: BCE_4066(malL)
BCZ: BCZK3772(malL)
BCB: BCB4264_A4121(malL)
BCU: BCAH820_4034(malL)
BCG: BCG9842_B1118(malL)
BCQ: BCQ_3804(malL)
BCX: BCA_4125(malL)
BCY: Bcer98_2716
BTK: BT9727_3756(malL)
BTL: BALH_3635(malL)
BWE: BcerKBAB4_3843
BLI: BL00491(malL)
BLD: BLi00664(malL)
OIH: OB2556
AFL: Aflv_2271(malL)
SHA: SH0072(malL)
LMO: lmo0184
LMF: LMOf2365_0195(malL-1) LMOf2365_0270(malL-2)
LMC: Lm4b_00181
LIN: lin0223
LWE: lwe0225(malL)
ESI: Exig_1739 Exig_2537
EAT: EAT1b_1266 EAT1b_1941
LLA: L128693(dexA)
LLM: llmg_0741(dexA)
LPL: lp_3627(agl6)
LJO: LJ0743
LSL: LSL_1712
LCA: LSEI_0406
LGA: LGAS_0518
LRE: Lreu_0083
OOE: OEOE_0040
LME: LEUM_0897
CBK: CLL_A0135
CBT: CLH_0118
CKL: CKL_1598(malL)
ATE: Athe_0165
CSC: Csac_2428
HOR: Hore_22530
MPU: MYPU_1030 MYPU_6330
MSY: MS53_0108
ART: Arth_0913
BLO: BL1526(agl)
BAD: BAD_1571(agl)
TDE: TDE0107
LIL: LA1466
RBA: RB2986
Taxonomy
Structures PDB: 1UOK  
Reference
  Authors
  Title

  Journal
  Organism
1  [PMID:291933]
Hauri HP, Quaroni A, Isselbacher KJ.
Biogenesis of intestinal plasma membrane: posttranslational route
and cleavage of sucrase-isomaltase.
Proc. Natl. Acad. Sci. U. S. A. 76 (1979) 5183-6.
Rattus norvegicus [GN:rno]
Reference
  Authors
  Title


  Journal
  Organism
2  [PMID:7002920]
Sjostrom H, Noren O, Christiansen L, Wacker H, Semenza G.
A fully active, two-active-site, single-chain sucrase.isomaltase
from pig small intestine. Implications for the biosynthesis of a
mammalian integral stalked membrane protein.
J. Biol. Chem. 255 (1980) 11332-8.
Sus scofa [GN:ssc]
Reference
  Authors
  Title

  Journal
  Organism
3  [PMID:6479163]
Rodriguez IR, Taravel FR, Whelan WJ.
Characterization and function of pig intestinal sucrase-isomaltase
and its separate subunits.
Eur. J. Biochem. 143 (1984) 575-82.
Sus scofa [GN:ssc]
Other DBs ExplorEnz - The Enzyme Database: 3.2.1.10
IUBMB Enzyme Nomenclature: 3.2.1.10
ExPASy - ENZYME nomenclature database: 3.2.1.10
BRENDA, the Enzyme Database: 3.2.1.10
CAS: 9032-15-9

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