KEGG   ENZYME: 3.2.1.48
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
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)
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
ec01110  Biosynthesis of secondary metabolites
Orthology
K01203  sucrase-isomaltase
Genes
HSA6476(SI)
PTR470988(SI)
PPS100973298(SI)
GGO101135022(SI)
PON100454405(SI)
PPYG129033434(SI)
NLE100585192(SI)
HMH116480289(SI)
SSYN134732951(SI)
MCC700840(SI)
MCF102128108(SI)
MTHB126947525
MNI105466450(SI)
CSAB103221316(SI)
CATY105586092(SI)
PANU101010666(SI)
TGE112618787(SI)
MLEU105535226(SI)
RRO104658581(SI)
RBB108540915(SI)
TFN117083676(SI)
PTEH111543532(SI)
CANG105513688(SI)
CJC100410281(SI)
SBQ101041197(SI)
CIMI108285818(SI)
ANAN105713612(SI)
CSYR103275008(SI)
MMUR105881524(SI)
LCAT123641648(SI)
OGA100959990(SI)
MMU69983(Sis)
MCAL110291317(Si)
MPAH110320350(Si)
RNO497756(Si)
MCOC116094065(Si)
ANU117707170(Si)
MUN110539420(Si)
CGE100773620(Si)
MAUA101823828(Si)
PROB127232655(Si)
PLEU114691704(Si)
MORG121452871(Si)
MFOT126504928
AAMP119826420(Si)
NGI103731721(Si)
HGL101711933(Si)
CPOC100731286(Si)
CCAN109679496(Si)
DORD105985553(Si)
DSP122107271(Si)
PLOP125351132(Si)
NCAR124993018
MMMA107149573(Si)
OCU100009093(SI)
OPI101520389(SI)
TUP102498900(SI)
GVR103597531(SI)
CFA488141(SI)
CLUD112645901(SI)
VVP112926645(SI)
VLG121477625(SI)
NPO129498671(SI)
AML100464408(SI)
UMR103664425(SI)
UAH113254160(SI)
UAR123801259(SI)
ELK111149399
LLV125099908
MPUF101676590(SI)
MNP132010108(SI)
MLK131824907(SI)
NVS122910467(SI)
ORO101381119(SI)
EJU114209109(SI)
ZCA113917271(SI)
MLX117999506(SI)
NSU110591708(SI)
LWW102741121(SI)
FCA100144605(SI)
PYU121033946(SI)
PCOO112849594(SI)
PBG122491769(SI)
PVIV125175012(SI)
LRUF124526713
PTG102964729(SI)
PPAD109262083(SI)
PUC125921182
AJU106987454
HHV120247215(SI)
BTA504366(SI)
BOM102268612(SI)
BIU109564411(SI)
BBUB102403856(SI)
BBIS104989290(SI)
CHX102187897(SI)
OAS101102774(SI)
BTAX128043833(SI)
CSUM138072862(SI)
ODA120869087(SI)
CCAD122444972(SI)
MREE136173261(SI)
MBEZ129551780(SI)
SSC100623884(SI)
CFR102523832(SI)
CBAI105066664(SI)
CDK105085981(SI)
VPC102527278(SI)
BACU103011824(SI)
BMUS118894529(SI)
LVE103080987(SI)
OOR101284967(SI)
DLE111174371(SI)
PCAD102981017(SI)
PSIU116753068(SI)
NASI112412120(SI)
ECB100063242(SI)
EPZ103566440(SI)
EAI106842405(SI)
MYB102254382(SI)
MYD102754902(SI)
MMYO118676712(SI)
MLF102435625(SI)
MDT132229150(SI)
PKL118723506(SI)
EFUS103286703(SI)
MNA107539283(SI)
DRO112304750(SI)
SHON118987514(SI)
AJM119046285(SI)
PDIC114490799(SI)
PHAS123827031(SI)
MMF118617283(SI)
PPAM129073206(SI)
RFQ117031133(SI)
PALE102885979(SI)
PGIG120598504(SI)
PVP105305949(SI)
RAY107519382(SI)
MJV108395638(SI)
TOD119258175(SI)
SARA101554601(SI)
LAV100666668(SI)
TMU101355803
ETF101654601(SI)
DNM101429055(SI)
MDO100013945(SI)
GAS123240281(SI)
SHR100932100(SI)
AFZ127552844
PCW110210220(SI)
TVP118847719(SI)
PBRV138157869(SI)
OAA100681776(SI)
BFO118427979
BBEL109466543 109485708
ARUN117298641
MNZ135205203
MRJ136855769
TSPTsp_01057
PVUL126813344
HRF124112471
HRJ124261832
HASI137269844 137270388 137281576 137281577 137281578
CVN111099718
MYI110459523
PMAX117342860
AIRR138308261
LJP135479549
LLON135494988
TADTRIADDRAFT_25103
 » show all
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)
DOI:10.1093/oxfordjournals.jbchem.a129048
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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