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)
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).
History
EC 3.2.1.48 created 1972
Pathway
ec00500  Starch and sucrose metabolism
ec01100  Metabolic pathways
Orthology
K01203  sucrase-isomaltase
Genes
HSA: 6476(SI)
PTR: 470988(SI)
PPS: 100973298(SI)
GGO: 101135022(SI)
PON: 100454405(SI)
NLE: 100585192(SI)
MCC: 700840(SI)
MCF: 102128108(SI)
CSAB: 103221316(SI)
RRO: 104658581(SI)
RBB: 108540915(SI)
CJC: 100410281(SI)
SBQ: 101041197(SI)
MMU: 69983(Sis)
RNO: 497756(Si)
CGE: 100773620(Si)
NGI: 103731721(Si)
HGL: 101711933(Si)
CCAN: 109679495 109679496(Si)
OCU: 100009093(SI)
TUP: 102498900(SI)
CFA: 488141(SI)
AML: 100464408(SI)
UMR: 103664425(SI)
ORO: 101381119(SI)
FCA: 100144605(SI)
PTG: 102964729(SI)
AJU: 106987454(SI)
BTA: 504366(SI)
BOM: 102268612(SI)
BIU: 109564411(SI)
PHD: 102329276(SI)
CHX: 102187897(SI)
OAS: 101102774(SI)
SSC: 100623884(SI)
CFR: 102523832(SI)
CDK: 105085981(SI)
BACU: 103011824(SI)
LVE: 103080987(SI)
OOR: 101284967(SI)
ECB: 100063242(SI)
EPZ: 103566440(SI)
EAI: 106842405(SI)
MYB: 102254382(SI)
MYD: 102754902(SI)
HAI: 109373269
RSS: 109438332(SI)
PALE: 102885979(SI)
LAV: 100666668(SI)
TMU: 101355803
MDO: 100013945(SI)
SHR: 100932100(SI)
OAA: 100681776(MGAM)
TSP: Tsp_01057
MYI: 110459523
LAK: 106164793
 » show all
Taxonomy
Reference
1  [PMID:807575]
  Authors
Conklin KA, Yamashiro KM, Gray GM.
  Title
Human intestinal sucrase-isomaltase. Identification of free sucrase and isomaltase and cleavage of the hybrid into active distinct subunits.
  Journal
J Biol Chem 250:5735-41 (1975)
Reference
2  [PMID:291933]
  Authors
Hauri HP, Quaroni A, Isselbacher KJ.
  Title
Biogenesis of intestinal plasma membrane: posttranslational route and cleavage of sucrase-isomaltase.
  Journal
Proc Natl Acad Sci U S A 76:5183-6 (1979)
DOI:10.1073/pnas.76.10.5183
Reference
3  [PMID:5073761]
  Authors
Kolinska J, Kraml J.
  Title
Separation and characterization of sucrose-isomaltase and of glucoamylase of rat intestine.
  Journal
Biochim Biophys Acta 284:235-47 (1972)
DOI:10.1016/0005-2744(72)90062-9
Reference
4  [PMID:1182172]
  Authors
Sigrist H, Ronner P, Semenza G.
  Title
A hydrophobic form of the small-intestinal sucrase-isomaltase complex.
  Journal
Biochim Biophys Acta 406:433-46 (1975)
DOI:10.1016/0005-2736(75)90022-X
Reference
5  [PMID:7002920]
  Authors
Sjostrom H, Noren O, Christiansen L, Wacker H, Semenza G.
  Title
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.
  Journal
J Biol Chem 255:11332-8 (1980)
Reference
6  [PMID:5804876]
  Authors
Takesue Y.
  Title
Purification and properties of rabbit intestinal sucrase.
  Journal
J Biochem (Tokyo) 65:545-52 (1969)
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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