KEGG   ENZYME: 3.2.1.48Help
Entry
EC 3.2.1.48                 Enzyme                                 

Name sucrose alpha-glucosidase;
sucrose alpha-glucohydrolase;
sucrase;
sucrase-isomaltase;
sucrose.alpha.-glucohydrolase;
intestinal sucrase;
sucrase(invertase)
Class Hydrolases;
Glycosylases;
Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
compounds
BRITE hierarchy
Sysname sucrose-alpha-D-glucohydrolase
Reaction(IUBMB) Hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type
action [RN:R00801 R06087]
Reaction(KEGG) R00801 R06087(G) > R00802 R06088(G)
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Comment This enzyme is isolated from intestinal mucosa as a single
polypeptide chain that also displays activity towards isomaltose (EC
3.2.1.10 oligo-1,6-glucosidase).
Pathway PATH: ec00500  Starch and sucrose metabolism
PATH: ec01100  Metabolic pathways
Orthology 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
Taxonomy
Structures PDB: 3CZE  3CZG  3CZK  3CZL  
Reference
  Authors
  Title


  Journal
  Organism
1  [PMID:807575]
Conklin KA, Yamashiro KM, Gray GM.
Human intestinal sucrase-isomaltase. Identification of free sucrase
and isomaltase and cleavage of the hybrid into active distinct
subunits.
J. Biol. Chem. 250 (1975) 5735-41.
Homo sapiens [GN:hsa]
Reference
  Authors
  Title

  Journal
  Organism
2  [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
3  [PMID:5073761]
Kolinska J, Kraml J.
Separation and characterization of sucrose-isomaltase and of
glucoamylase of rat intestine.
Biochim. Biophys. Acta. 284 (1972) 235-47.
Rattus norvegicus [GN:rno]
Reference
  Authors
  Title

  Journal
  Organism
4  [PMID:1182172]
Sigrist H, Ronner P, Semenza G.
A hydrophobic form of the small-intestinal sucrase-isomaltase
complex.
Biochim. Biophys. Acta. 406 (1975) 433-46.
Oryctolagus cuniculus
Reference
  Authors
  Title


  Journal
  Organism
5  [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
6  [PMID:5804876]
Takesue Y.
Purification and properties of rabbit intestinal sucrase.
J. Biochem. (Tokyo). 65 (1969) 545-52.
Oryctolagus cuniculus
Other DBs ExplorEnz - The Enzyme Database: 3.2.1.48
IUBMB Enzyme Nomenclature: 3.2.1.48
ExPASy - ENZYME nomenclature database: 3.2.1.48
BRENDA, the Enzyme Database: 3.2.1.48
CAS: 37288-39-4

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