Biotin—(methylmalonyl-CoA-carboxytransferase) ligase
In enzymology, a biotin-[methylmalonyl-CoA-carboxytransferase] ligase (EC 6.3.4.9) is an enzyme that catalyzes the chemical reaction
- ATP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxytransferase] AMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxytransferase]
The 3 substrates of this enzyme are ATP, biotin, and [[apo-[methylmalonyl-CoA:pyruvate carboxytransferase]]], whereas its 3 products are AMP, diphosphate, and methylmalonyl-CoA:pyruvate carboxytransferase.
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of this enzyme class is biotin:apo[methylmalonyl-CoA:pyruvate carboxytransferase] ligase (AMP-forming). Other names in common use include biotin-[methylmalonyl-CoA-carboxyltransferase] synthetase, biotin-methylmalonyl coenzyme A carboxyltransferase synthetase, biotin-transcarboxylase synthetase, methylmalonyl coenzyme A holotranscarboxylase synthetase, biotin-[methylmalonyl-CoA-carboxyltransferase] ligase, biotin:apo[methylmalonyl-CoA:pyruvate carboxyltransferase] ligase, and (AMP-forming). This enzyme participates in biotin metabolism.
References
- Lane MD, Young DL and Lynen F (1964). "The enzymatic synthesis of holotranscarboxylase from apotranscarboxylase and (+)-biotin. I. Purification of the apoenzyme and synthetase; characteristics of the reaction". J. Biol. Chem. 239: 2858–2864.
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| 6.1: Carbon-Oxygen | |
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| 6.2: Carbon-Sulfur | |
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| 6.3: Carbon-Nitrogen | |
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