Sequence of MGA_HUMAN
EC Number:3.2.1
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
Other sequences found for EC No. 3.2.1
EC Number:3.2.1.3
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
Other sequences found for EC No. 3.2.1.3
EC Number:3.2.1.20
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
maltotetraose + 3 H2O = 4 alpha-D-glucose
Other sequences found for EC No. 3.2.1.20
General information:
Sequence
0 MARKKLKKFT TLEIVLSVLL LVLFIISIVL IVLLAKESLK STAPDPGTTG TPDPGTTGTP
60 DPGTTGTTHA RTTGPPDPGT TGTTPVSAEC PVVNELERIN CIPDQPPTKA TCDQRGCCWN
120 PQGAVSVPWC YYSKNHSYHV EGNLVNTNAG FTARLKNLPS SPVFGSNVDN VLLTAEYQTS
180 NRFHFKLTDQ TNNRFEVPHE HVQSFSGNAA ASLTYQVEIS RQPFSIKVTR RSNNRVLFDS
240 SIGPLLFADQ FLQLSTRLPS TNVYGLGEHV HQQYRHDMNW KTWPIFNRDT TPNGNGTNLY
300 GAQTFFLCLE DASGLSFGVF LMNSNAMEVV LQPAPAITYR TIGGILDFYV FLGNTPEQVV
360 QEYLELIGRP ALPSYWALGF HLSRYEYGTL DNMREVVERN RAAQLPYDVQ HADIDYMDER
420 RDFTYDSVDF KGFPEFVNEL HNNGQKLVII VDPAISNNSS SSKPYGPYDR GSDMKIWVNS
480 SDGVTPLIGE VWPGQTVFPD YTNPNCAVWW TKEFELFHNQ VEFDGIWIDM NEVSNFVDGS
540 VSGCSTNNLN NPPFTPRILD GYLFCKTLCM DAVQHWGKQY DIHNLYGYSM AVATAEAAKT
600 VFPNKRSFIL TRSTFAGSGK FAAHWLGDNT ATWDDLRWSI PGVLEFNLFG IPMVGPDICG
660 FALDTPEELC RRWMQLGAFY PFSRNHNGQG YKDQDPASFG ADSLLLNSSR HYLNIRYTLL
720 PYLYTLFFRA HSRGDTVARP LLHEFYEDNS TWDVHQQFLW GPGLLITPVL DEGAEKVMAY
780 VPDAVWYDYE TGSQVRWRKQ KVEMELPGDK IGLHLRGGYI FPTQQPNTTT LASRKNPLGL
840 IIALDENKEA KGELFWDNGE TKDTVANKVY LLCEFSVTQN RLEVNISQST YKDPNNLAFN
900 EIKILGTEEP SNVTVKHNGV PSQTSPTVTY DSNLKVAIIT DIDLLLGEAY TVEWSIKIRD
960 EEKIDCYPDE NGASAENCTA RGCIWEASNS SGVPFCYFVN DLYSVSDVQY NSHGATADIS
1020 LKSSVYANAF PSTPVNPLRL DVTYHKNEML QFKIYDPNKN RYEVPVPLNI PSMPSSTPEG
1080 QLYDVLIKKN PFGIEIRRKS TGTIIWDSQL LGFTFSDMFI RISTRLPSKY LYGFGETEHR
1140 SYRRDLEWHT WGMFSRDQPP GYKKNSYGVH PYYMGLEEDG SAHGVLLLNS NAMDVTFQPL
1200 PALTYRTTGG VLDFYVFLGP TPELVTQQYT ELIGRPVMVP YWSLGFQLCR YGYQNDSEIA
1260 SLYDEMVAAQ IPYDVQYSDI DYMERQLDFT LSPKFAGFPA LINRMKADGM RVILILDPAI
1320 SGNETQPYPA FTRGVEDDVF IKYPNDGDIV WGKVWPDFPD VVVNGSLDWD SQVELYRAYV
1380 AFPDFFRNST AKWWKREIEE LYNNPQNPER SLKFDGMWID MNEPSSFVNG AVSPGCRDAS
1440 LNHPPYMPHL ESRDRGLSSK TLCMESQQIL PDGSLVQHYN VHNLYGWSQT RPTYEAVQEV
1500 TGQRGVVITR STFPSSGRWA GHWLGDNTAA WDQLKKSIIG MMEFSLFGIS YTGADICGFF
1560 QDAEYEMCVR WMQLGAFYPF SRNHNTIGTR RQDPVSWDAA FVNISRNVLQ TRYTLLPYLY
1620 TLMQKAHTEG VTVVRPLLHE FVSDQVTWDI DSQFLLGPAF LVSPVLERNA RNVTAYFPRA
1680 RWYDYYTGVD INARGEWKTL PAPLDHINLH VRGGYILPWQ EPALNTHLSR KNPLGLIIAL
1740 DENKEAKGEL FWDDGQTKDT VAKKVYLLCE FSVTQNHLEV TISQSTYKDP NNLAFNEIKI
1800 LGMEEPSNVT VKHNGVPSQT SPTVTYDSNL KVAIITDINL FLGEAYTVEW SIKIRDEEKI
1860 DCYPDENGDS AENCTARGCI WEASNSSGVP FCYFVNDLYS VSDVQYNSHG ATADISLKSS
1920 VHANAFPSTP VNPLRLDVTY HKNEMLQFKI YDPNNNRYEV PVPLNIPSVP SSTPEGQLYD
1980 VLIKKNPFGI EIRRKSTGTI IWDSQLLGFT FNDMFIRIST RLPSKYLYGF GETEHTSYRR
2040 DLEWHTWGMF SRDQPPGYKK NSYGVHPYYM GLEEDGSAHG VLLLNSNAMD VTFQPLPALT
2100 YRTTGGVLDF YVFLGPTPEL VTQQYTELIG RPVMVPYWSL GFQLCRYGYQ NDSEISSLYD
2160 EMVAAQIPYD VQYSDIDYME RQLDFTLSPK FAGFPALINR MKADGMRVIL ILDPAISGNE
2220 TQPYPAFTRG VEDDVFIKYP NDGDIVWGKV WPDFPDVVVN GSLDWDSQVE LYRAYVAFPD
2280 FFRNSTAKWW KREIEELYNN PQNPERSLKF DGMWIDMNEP SSFVNGAVSP GCRDASLNHP
2340 PYMPYLESRD RGLSSKTLCM ESQQILPDGS PVQHYNVHNL YGWSQTRPTY EAVQEVTGQR
2400 GVVITRSTFP SSGRWAGHWL GDNTAAWDQL KKSIIGMMEF SLFGISYTGA DICGFFQDAE
2460 YEMCVRWMQL GAFYPFSRNH NTIGTRRQDP VSWDVAFVNI SRTVLQTRYT LLPYLYTLMH
2520 KAHTEGVTVV RPLLHEFVSD QVTWDIDSQF LLGPAFLVSP VLERNARNVT AYFPRARWYD
2580 YYTGVDINAR GEWKTLPAPL DHINLHVRGG YILPWQEPAL NTHLSRQKFM GFKIALDDEG
2640 TAGGWLFWDD GQSIDTYGKG LYYLASFSAS QNTMQSHIIF NNYITGTNPL KLGYIEIWGV
2700 GSVPVTSVSI SVSGMVITPS FNNDPTTQVL SIDVTDRNIS LHNFTSLTWI STL
Download this sequence
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
696547
Nichols B.L.,Eldering J.A.,Avery S.E.,Hahn D.,Quaroni A.,Sterchi E.E.
Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase.
J. Biol. Chem.
273
3076-3081
1998
696549
Hillier L.W.,Fulton R.S.,Fulton L.A.,Graves T.A.,Pepin K.H.,Wagner-McPherson C.,Layman D.,Maas J.,Jaeger S.,Walker R.,Wylie K.,Sekhon M.,Becker M.C.,O'Laughlin M.D.,Schaller M.E.,Fewell G.A.,Delehaunty K.D.,Miner T.L.,Nash W.E.,Cordes M.,Du H.,Sun H.,Edwards J.,Bradshaw-Cordum H.,Ali J.,Andrews S.,Isak A.,Vanbrunt A.,Nguyen C.,Du F.,Lamar B.,Courtney L.,Kalicki J.,Ozersky P.,Bielicki L.,Scott K.,Holmes A.,Harkins R.,Harris A.,Strong C.M.,Hou S.,Tomlinson C.,Dauphin-Kohlberg S.,Kozlowicz-Reilly A.,Leonard S.,Rohlfing T.,Rock S.M.,Tin-Wollam A.-M.,Abbott A.,Minx P.,Maupin R.,Strowmatt C.,Latreille P.,Miller N.,Johnson D.,Murray J.,Woessner J.P.,Wendl M.C.,Yang S.-P.,Schultz B.R.,Wallis J.W.,Spieth J.,Bieri T.A.,Nelson J.O.,Berkowicz N.,Wohldmann P.E.,Cook L.L.,Hickenbotham M.T.,Eldred J.,Williams D.,Bedell J.A.,Mardis E.R.,Clifton S.W.,Chissoe S.L.,Marra M.A.,Raymond C.,Haugen E.,Gillett W.,Zhou Y.,James R.,Phelps K.,Iadanoto S.,Bubb K.,Simms E.,Levy R.,Clendenning J.,Kaul R.,Kent W.J.,Furey T.S.,Baertsch R.A.,Brent M.R.,Keibler E.,Flicek P.,Bork P.,Suyama M.,Bailey J.A.,Portnoy M.E.,Torrents D.,Chinwalla A.T.,Gish W.R.,Eddy S.R.,McPherson J.D.,Olson M.V.,Eichler E.E.,Green E.D.,Waterston R.H.,Wilson R.K.
The DNA sequence of human chromosome 7.
Nature
424
157-164
2003
696550
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
696551
Fagerberg L.,Hallstroem B.M.,Oksvold P.,Kampf C.,Djureinovic D.,Odeberg J.,Habuka M.,Tahmasebpoor S.,Danielsson A.,Edlund K.,Asplund A.,Sjoestedt E.,Lundberg E.,Szigyarto C.A.,Skogs M.,Takanen J.O.,Berling H.,Tegel H.,Mulder J.,Nilsson P.,Schwenk J.M.,Lindskog C.,Danielsson F.,Mardinoglu A.,Sivertsson A.,von Feilitzen K.,Forsberg M.,Zwahlen M.,Olsson I.,Navani S.,Huss M.,Nielsen J.,Ponten F.,Uhlen M.
Analysis of the human tissue-specific expression by genome-wide integration of transcriptomics and antibody-based proteomics.
Mol. Cell. Proteomics
13
397-406
2014
696552
Danielsen E.M.
Tyrosine sulfation, a post-translational modification of microvillar enzymes in the small intestinal enterocyte.
EMBO J.
6
2891-2896
1987
696553
Naim H.Y.,Sterchi E.E.,Lentze M.J.
Structure, biosynthesis, and glycosylation of human small intestinal maltase-glucoamylase.
J. Biol. Chem.
263
19709-19717
1988
696554
Nichols B.L.,Avery S.,Sen P.,Swallow D.M.,Hahn D.,Sterchi E.
The maltase-glucoamylase gene: common ancestry to sucrase-isomaltase with complementary starch digestion activities.
Proc. Natl. Acad. Sci. U.S.A.
100
1432-1437
2003
696555
Quezada-Calvillo R.,Sim L.,Ao Z.,Hamaker B.R.,Quaroni A.,Brayer G.D.,Sterchi E.E.,Robayo-Torres C.C.,Rose D.R.,Nichols B.L.
Luminal starch substrate brake on maltase-glucoamylase activity is located within the glucoamylase subunit.
J. Nutr.
138
685-692
2008
696556
Ren L.,Qin X.,Cao X.,Wang L.,Bai F.,Bai G.,Shen Y.
Structural insight into substrate specificity of human intestinal maltase-glucoamylase.
Protein Cell
2
827-836
2011
696557
Lee B.H.,Rose D.R.,Lin A.H.,Quezada-Calvillo R.,Nichols B.L.,Hamaker B.R.
Contribution of the Individual Small Intestinal alpha-Glucosidases to Digestion of Unusual alpha-Linked Glycemic Disaccharides.
J. Agric. Food Chem.
64
6487-6494
2016
696558
Sim L.,Quezada-Calvillo R.,Sterchi E.E.,Nichols B.L.,Rose D.R.
Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.
J. Mol. Biol.
375
782-792
2008
