MLYCD

Malonyl-CoA decarboxylase, mitochondrial

504 amino acids

Catalyzes the conversion of malonyl-CoA to acetyl-CoA. In the fatty acid biosynthesis MCD selectively removes malonyl-CoA and thus assures that methyl-malonyl-CoA is the only chain elongating substrate for fatty acid synthase and that fatty acids with multiple methyl side chains are produced.

56.69 kDa

MRGLRRGLSRLGPRLGPWAVPRSLRRVLRAAGPWRGQSSAGSVSERGGASMEEVLSRSVPLLPPYETKEKAPPPAERRSAEFVRYYRGLEAGSRRAELLGCLARDFGADHGRVAEFSAKVLQAREQEREQGALLQAEDRVRYYLTPRYRALFQHLGRLEGGLRFLVELRGDLVEGLAAKAVDGPHVKEMSGVLKNMLSEWFSTGFLNLERVTWQSPCEVLQKISDSEAVHPVRNWVDLKRRVGPYRRCYFFSHCAIPGEPLIILHVALTSDISSSIQSIVKDVESLETEDAEKITTAIFYSISLAQQGLQGVELGNHLIKRVVKELQKDLPQIEAFSSLSPIPGFTKWLVGLLSSQTKELGRNELFTESERQEISEITEDSTTETLKKLLTNSEWVKSEKLVKALHSPLMRLCAWYLYGEKHRGYALNPVANFHLQNGAELWRINWMGDTSPRGIAASCGMMVNYRYFLEDTASNSAAYLGTKHIKASEQVLSFVSQFQQNSKL

MLYCD

Malonyl-CoA decarboxylase, mitochondrial

493 amino acids

Catalyzes the conversion of malonyl-CoA to acetyl-CoA. In the fatty acid biosynthesis MCD selectively removes malonyl-CoA and thus assures that methyl-malonyl-CoA is the only chain elongating substrate for fatty acid synthase and that fatty acids with multiple methyl side chains are produced. In peroxisomes it may be involved in degrading intraperoxisomal malonyl-CoA, which is generated by the peroxisomal beta-oxidation of odd chain-length dicarboxylic fatty acids. Plays a role in the metabolic balance between glucose and lipid oxidation in muscle independent of alterations in insulin signaling. May play a role in controlling the extent of ischemic injury by promoting glucose oxidation.

55.003 kDa

MRGFGPGLTARRLLPLRLPPRPPGPRLASGQAAGALERAMDELLRRAVPPTPAYELREKTPAPAEGQCADFVSFYGGLAETAQRAELLGRLARGFGVDHGQVAEQSAGVLHLRQQQREAAVLLQAEDRLRYALVPRYRGLFHHISKLDGGVRFLVQLRADLLEAQALKLVEGPDVREMNGVLKGMLSEWFSSGFLNLERVTWHSPCEVLQKISEAEAVHPVKNWMDMKRRVGPYRRCYFFSHCSTPGEPLVVLHVALTGDISSNIQAIVKEHPPSETEEKNKITAAIFYSISLTQQGLQGVELGTFLIKRVVKELQREFPHLGVFSSLSPIPGFTKWLLGLLNSQTKEHGRNELFTDSECKEISEITGGPINETLKLLLSSSEWVQSEKLVRALQTPLMRLCAWYLYGEKHRGYALNPVANFHLQNGAVLWRINWMADVSLRGITGSCGLMANYRYFLEETGPNSTSYLGSKIIKASEQVLSLVAQFQKNSKL

Mlycd

Malonyl-CoA decarboxylase, mitochondrial

492 amino acids

Catalyzes the conversion of malonyl-CoA to acetyl-CoA. In the fatty acid biosynthesis MCD selectively removes malonyl-CoA and thus assures that methyl-malonyl-CoA is the only chain elongating substrate for fatty acid synthase and that fatty acids with multiple methyl side chains are produced. In peroxisomes it may be involved in degrading intraperoxisomal malonyl-CoA, which is generated by the peroxisomal beta-oxidation of odd chain-length dicarboxylic fatty acids. Plays a role in the metabolic balance between glucose and lipid oxidation in muscle independent of alterations in insulin signaling. Plays a role in controlling the extent of ischemic injury by promoting glucose oxidation.

54.736 kDa

MRGLGPGLRARRLLPLRSPPRPPGPRGRRLCGGLAASAMDELLRRAVPPTPAYELREKTPAPAEGQCADFVSFYGGLAEASQRAELLGRLAQGFGVDHGQVAEQSAGVLQLRQQAREAAVLLQAEDRLRYALVPRYRGLFHHISKLDGGVRFLVQLRADLLEAQALKLVEGPHVREMNGVLKSMLSEWFSSGFLNLERVTWHSPCEVLQKISECEAVHPVKNWMDMKRRVGPYRRCYFFSHCSTPGEPLVVLHVALTGDISNNIQGIVKECPPTETEERNRIAAAIFYSISLTQQGLQGVELGTFLIKRVVKELQKEFPQLGAFSSLSPIPGFTKWLLGLLNVQGKEHGRNELFTDSECQEISAVTGNPVHESLKGFLSSGEWVKSEKLTQALQGPLMRLCAWYLYGEKHRGYALNPVANFHLQNGAVMWRINWMADSSLKGLTSSCGLMVNYRYYLEETGPNSISYLGSKNIKASEQILSLVAQFQNNSKL

Mlycd

Malonyl-CoA decarboxylase, mitochondrial

492 amino acids

Catalyzes the conversion of malonyl-CoA to acetyl-CoA. In the fatty acid biosynthesis MCD selectively removes malonyl-CoA and thus assures that methyl-malonyl-CoA is the only chain elongating substrate for fatty acid synthase and that fatty acids with multiple methyl side chains are produced. In peroxisomes it may be involved in degrading intraperoxisomal malonyl-CoA, which is generated by the peroxisomal beta-oxidation of odd chain-length dicarboxylic fatty acids. Plays a role in the metabolic balance between glucose and lipid oxidation in muscle independent of alterations in insulin signaling. May play a role in controlling the extent of ischemic injury by promoting glucose oxidation.

54.762 kDa

MRGLGPSLRARRLLPLRYPPRPPGPRGPRLCSGLTASAMDELLRRAVPPTPAYELREKTPAPAEGQCADFVSFYGGLAEAAQRAELLGRLAQGFGVDHGQVAEQSAGVLQLRQQSREAAVLLQAEDRLRYALVPRYRGLFHHISKLDGGVRFLVQLRADLLEAQALKLVEGPHVREMNGVLKSMLSEWFSSGFLNLERVTWHSPCEVLQKISECEAVHPVKNWMDMKRRVGPYRRCYFFSHCSTPGDPLVVLHVALTGDISNNIQSIVKECPPSETEEKNRIAAAVFYSISLTQQGLQGVELGTFLIKRVVKELQKEFPHLGAFSSLSPIPGFTKWLLGLLNVQGKEYGRNELFTDSECKEIAEVTGDPVHESLKGLLSSGEWAKSEKLAQALQGPLMRLCAWYLYGEKHRGYALNPVANFHLQNGAVMWRINWMADSSLKGLTSSCGLMVNYRYYLEETGPNSISYLGSKNIKASEQILSLVAQFQSNSKL