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Acetyl co-enzyme A carboxylase carboxyltransferase-like
Acetyl co-enzyme A carboxylase carboxyltransferase is composed of an alpha and beta subunit. This protein family includes the alpha subunit and similar sequences. [1]. 10470374. The regulation of acetyl-CoA carboxylase--a potential target for the action of hypolipidemic agents. Munday MR, Hemingway CJ;. Adv Enzyme Regul 1999;39:205-234. (from Pfam)
carboxyl transferase domain-containing protein
All of the members in this family are biotin dependent carboxylases. The carboxyl transferase domain carries out the following reaction; transcarboxylation from biotin to an acceptor molecule. There are two recognised types of carboxyl transferase. One of them uses acyl-CoA and the other uses 2-oxoacid as the acceptor molecule of carbon dioxide. All of the members in this family utilise acyl-CoA as the acceptor molecule. [1]. 8366018. Primary structure of the monomer of the 12S subunit of transcarboxylase as deduced from DNA and characterization of the product expressed in Escherichia coli. Thornton CG, Kumar GK, Haase FC, Phillips NF, Woo SB, Park VM, Magner WJ, Shenoy BC, Wood HG, Samols D;. J Bacteriol 1993;175:5301-5308. [2]. 8102604. Molecular evolution of biotin-dependent carboxylases. Toh H, Kondo H, Tanabe T;. Eur J Biochem 1993;215:687-696. [3]. 12663926. Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase. Zhang H, Yang Z, Shen Y, Tong L;. Science 2003;299:2064-2067. (from Pfam)
biotin carboxylase N-terminal domain-containing protein
This domain is structurally related to the PreATP-grasp domain. The family contains the N-terminus of biotin carboxylase enzymes [1,3], and propionyl-CoA carboxylase A chain [2]. [1]. 7915138. Three-dimensional structure of the biotin carboxylase subunit. of acetyl-CoA carboxylase. Waldrop GL, Rayment I, Holden HM;. Biochemistry 1994;33:10249-10256. [2]. 25383525. Structure and function of a single-chain, multi-domain long-chain acyl-CoA carboxylase. Tran TH, Hsiao YS, Jo J, Chou CY, Dietrich LE, Walz T, Tong L;. Nature. 2015;518:120-124. [3]. 20443544. Structural impact of human and Escherichia coli biotin carboxyl carrier proteins on biotin attachment. Healy S, McDonald MK, Wu X, Yue WW, Kochan G, Oppermann U, Gravel RA;. Biochemistry. 2010;49:4687-4694. (from Pfam)
carboxyltransferase subunit alpha
acetyl-CoA carboxylase carboxyltransferase subunit alpha
acetyl-coenzyme A carboxylase carboxyl transferase subunits beta/alpha
acetyl-coenzyme A carboxylase carboxyl transferase subunits beta/alpha is a component of the acetyl coenzyme A carboxylase (ACC) complex that catalyzes the carboxylation of acetyl-CoA to form malonyl-CoA
acetyl-CoA carboxylase carboxyl transferase subunit alpha
The enzyme acetyl-CoA carboxylase contains a biotin carboxyl carrier protein or domain, a biotin carboxylase, and a carboxyl transferase. This model represents the alpha chain of the carboxyl transferase for cases in which the architecture of the protein is as in E. coli, in which the carboxyltransferase portion consists of two non-identical subnits, alpha and beta.
acetyl-CoA carboxylase, carboxyltransferase subunit beta
The enzyme acetyl-CoA carboxylase contains a biotin carboxyl carrier protein or domain, a biotin carboxylase, and a carboxyl transferase. This model represents the beta chain of the carboxyl transferase for cases in which the architecture of the protein is as in E. coli, in which the carboxyltransferase portion consists of two non-identical subnits, alpha and beta.
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