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Sequence of DCMC_HUMAN

EC Number:4.1.1.9

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
malonyl-CoA decarboxylase
O95822
Homo sapiens
493
55003
Reaction
malonyl-CoA = acetyl-CoA + CO2
Other sequences found for EC No. 4.1.1.9

General information:

Sequence
show sequence in fasta format
  0 MRGFGPGLTA RRLLPLRLPP RPPGPRLASG QAAGALERAM DELLRRAVPP TPAYELREKT
 60 PAPAEGQCAD FVSFYGGLAE TAQRAELLGR LARGFGVDHG QVAEQSAGVL HLRQQQREAA
120 VLLQAEDRLR YALVPRYRGL FHHISKLDGG VRFLVQLRAD LLEAQALKLV EGPDVREMNG
180 VLKGMLSEWF SSGFLNLERV TWHSPCEVLQ KISEAEAVHP VKNWMDMKRR VGPYRRCYFF
240 SHCSTPGEPL VVLHVALTGD ISSNIQAIVK EHPPSETEEK NKITAAIFYS ISLTQQGLQG
300 VELGTFLIKR VVKELQREFP HLGVFSSLSP IPGFTKWLLG LLNSQTKEHG RNELFTDSEC
360 KEISEITGGP INETLKLLLS SSEWVQSEKL VRALQTPLMR LCAWYLYGEK HRGYALNPVA
420 NFHLQNGAVL WRINWMADVS LRGITGSCGL MANYRYFLEE TGPNSTSYLG SKIIKASEQV
480 LSLVAQFQKN SKL
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
283002
FitzPatrick D.R.,Hill A.,Tolmie J.L.,Thorburn D.R.,Christodoulou J.
The molecular basis of malonyl-CoA decarboxylase deficiency.
Am. J. Hum. Genet.
65
318-326
1999
283003
Sacksteder K.A.,Morrell J.C.,Wanders R.J.A.,Matalon R.,Gould S.J.
MCD encodes peroxisomal and cytoplasmic forms of malonyl-CoA decarboxylase and is mutated in malonyl-CoA decarboxylase deficiency.
J. Biol. Chem.
274
24461-24468
1999
283004
Gao J.,Waber L.,Bennett M.J.,Gibson K.M.,Cohen J.C.
Cloning and mutational analysis of human malonyl-coenzyme A decarboxylase.
J. Lipid Res.
40
178-182
1999
283005
Martin J.,Han C.,Gordon L.A.,Terry A.,Prabhakar S.,She X.,Xie G.,Hellsten U.,Chan Y.M.,Altherr M.,Couronne O.,Aerts A.,Bajorek E.,Black S.,Blumer H.,Branscomb E.,Brown N.C.,Bruno W.J.,Buckingham J.M.,Callen D.F.,Campbell C.S.,Campbell M.L.,Campbell E.W.,Caoile C.,Challacombe J.F.,Chasteen L.A.,Chertkov O.,Chi H.C.,Christensen M.,Clark L.M.,Cohn J.D.,Denys M.,Detter J.C.,Dickson M.,Dimitrijevic-Bussod M.,Escobar J.,Fawcett J.J.,Flowers D.,Fotopulos D.,Glavina T.,Gomez M.,Gonzales E.,Goodstein D.,Goodwin L.A.,Grady D.L.,Grigoriev I.,Groza M.,Hammon N.,Hawkins T.,Haydu L.,Hildebrand C.E.,Huang W.,Israni S.,Jett J.,Jewett P.B.,Kadner K.,Kimball H.,Kobayashi A.,Krawczyk M.-C.,Leyba T.,Longmire J.L.,Lopez F.,Lou Y.,Lowry S.,Ludeman T.,Manohar C.F.,Mark G.A.,McMurray K.L.,Meincke L.J.,Morgan J.,Moyzis R.K.,Mundt M.O.,Munk A.C.,Nandkeshwar R.D.,Pitluck S.,Pollard M.,Predki P.,Parson-Quintana B.,Ramirez L.,Rash S.,Retterer J.,Ricke D.O.,Robinson D.L.,Rodriguez A.,Salamov A.,Saunders E.H.,Scott D.,Shough T.,Stallings R.L.,Stalvey M.,Sutherland R.D.,Tapia R.,Tesmer J.G.,Thayer N.,Thompson L.S.,Tice H.,Torney D.C.,Tran-Gyamfi M.,Tsai M.,Ulanovsky L.E.,Ustaszewska A.,Vo N.,White P.S.,Williams A.L.,Wills P.L.,Wu J.-R.,Wu K.,Yang J.,DeJong P.,Bruce D.,Doggett N.A.,Deaven L.,Schmutz J.,Grimwood J.,Richardson P.,Rokhsar D.S.,Eichler E.E.,Gilna P.,Lucas S.M.,Myers R.M.,Rubin E.M.,Pennacchio L.A.
The sequence and analysis of duplication-rich human chromosome 16.
Nature
432
988-994
2004
283006
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
283007
Zhou D.,Yuen P.,Chu D.,Thon V.,McConnell S.,Brown S.,Tsang A.,Pena M.,Russell A.,Cheng J.F.,Nadzan A.M.,Barbosa M.S.,Dyck J.R.,Lopaschuk G.D.,Yang G.
Expression, purification, and characterization of human malonyl-CoA decarboxylase.
Protein Expr. Purif.
34
261-269
2004
283008
Bouzakri K.,Austin R.,Rune A.,Lassman M.E.,Garcia-Roves P.M.,Berger J.P.,Krook A.,Chibalin A.V.,Zhang B.B.,Zierath J.R.
Malonyl CoenzymeA decarboxylase regulates lipid and glucose metabolism in human skeletal muscle.
Diabetes
57
1508-1516
2008
283009
Ghosh D.,Berg J.M.
A proteome-wide perspective on peroxisome targeting signal 1(PTS1)-Pex5p affinities.
J. Am. Chem. Soc.
132
3973-3979
2010
283010
Vaca Jacome A.S.,Rabilloud T.,Schaeffer-Reiss C.,Rompais M.,Ayoub D.,Lane L.,Bairoch A.,Van Dorsselaer A.,Carapito C.
N-terminome analysis of the human mitochondrial proteome.
Proteomics
15
2519-2524
2015
283011
Aparicio D.,Perez R.,Carpena X.,Diaz M.,Ferrer J.C.,Loewen P.C.,Fita I.
Structural asymmetry and disulphide bridges among subunits modulate the activity of human Malonyl-CoA Decarboxylase.
J. Biol. Chem.
288
11907-11919
2013
283012
Froese D.S.,Forouhar F.,Tran T.H.,Vollmar M.,Kim Y.S.,Lew S.,Neely H.,Seetharaman J.,Shen Y.,Xiao R.,Acton T.B.,Everett J.K.,Cannone G.,Puranik S.,Savitsky P.,Krojer T.,Pilka E.S.,Kiyani W.,Lee W.H.,Marsden B.D.,von Delft F.,Allerston C.K.,Spagnolo L.,Gileadi O.,Montelione G.T.,Oppermann U.,Yue W.W.,Tong L.
Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations.
Structure
21
1182-1192
2013