Malonyl-S-ACP:biotin-protein carboxyltransferase

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Malonyl-S-ACP:biotin-protein carboxyltransferase
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EC no. 2.1.3.10
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Malonyl-S-ACP:biotin-protein carboxyltransferase (EC 2.1.3.10, malonyl-S-acyl-carrier protein:biotin-protein carboxyltransferase, MadC/MadD, MadC,D, malonyl-[acyl-carrier protein]:biotinyl-[protein] carboxyltransferase) is an enzyme with systematic name malonyl-(acyl-carrier protein):biotinyl-(protein) carboxytransferase. [1] [2] [3] This enzyme catalyses the following chemical reaction

malonyl-[acyl-carrier protein] + biotinyl-[protein] acetyl-[acyl-carrier protein] + carboxybiotinyl-[protein]

This enzyme is a component of EC 4.1.1.89, biotin-dependent malonate decarboxylase.

Related Research Articles

<span class="mw-page-title-main">Malonyl-CoA</span> Chemical compound

Malonyl-CoA is a coenzyme A derivative of malonic acid.

<span class="mw-page-title-main">Oxaloacetate decarboxylase</span> Enzyme

Oxaloacetate decarboxylase is a carboxy-lyase involved in the conversion of oxaloacetate into pyruvate.

<span class="mw-page-title-main">Beta-ketoacyl-ACP synthase</span> Enzyme

In molecular biology, Beta-ketoacyl-ACP synthase EC 2.3.1.41, is an enzyme involved in fatty acid synthesis. It typically uses malonyl-CoA as a carbon source to elongate ACP-bound acyl species, resulting in the formation of ACP-bound β-ketoacyl species such as acetoacetyl-ACP.

<span class="mw-page-title-main">Methylmalonyl-CoA carboxytransferase</span>

In enzymology, a methylmalonyl-CoA carboxytransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Biotin carboxylase</span> Class of enzymes

In enzymology, a biotin carboxylase (EC 6.3.4.14) is an enzyme that catalyzes the chemical reaction

In enzymology, a [acyl-carrier-protein] S-acetyltransferase is an enzyme that catalyzes the reversible chemical reaction

In enzymology, a [acyl-carrier-protein] S-malonyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a beta-ketoacyl-acyl-carrier-protein synthase I is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Fatty-acyl-CoA synthase</span>

Fatty-acyl-CoA Synthase, or more commonly known as yeast fatty acid synthase, is an enzyme complex responsible for fatty acid biosynthesis, and is of Type I Fatty Acid Synthesis (FAS). Yeast fatty acid synthase plays a pivotal role in fatty acid synthesis. It is a 2.6 MDa barrel shaped complex and is composed of two, unique multi-functional subunits: alpha and beta. Together, the alpha and beta units are arranged in an α6β6 structure. The catalytic activities of this enzyme complex involves a coordination system of enzymatic reactions between the alpha and beta subunits. The enzyme complex therefore consists of six functional centers for fatty acid synthesis.

<span class="mw-page-title-main">MCAT (gene)</span> Protein-coding gene in the species Homo sapiens

Malonyl CoA-acyl carrier protein transacylase, mitochondrial is an enzyme that in humans is encoded by the MCAT gene.

Acetyl-S-ACP:malonate ACP transferase is an enzyme with systematic name acetyl-(acyl-carrier-protein):malonate S-(acyl-carrier-protein)transferase. This enzyme catalyses the following chemical reaction

Malonate decarboxylase holo-(acyl-carrier protein) synthase is an enzyme with systematic name 2'-(5-triphosphoribosyl)-3'-dephospho-CoA:apo-malonate-decarboxylase 2'-(5-phosphoribosyl)-3'-dephospho-CoA-transferase . This enzyme catalyses the following chemical reaction

Malonyl-S-ACP decarboxylase (EC 4.1.1.87, malonyl-S-acyl-carrier protein decarboxylase, MdcD/MdcE, MdcD,E) is an enzyme with systematic name malonyl-(acyl-carrier-protein) carboxy-lyase. This enzyme catalyses the following chemical reaction

Biotin-independent malonate decarboxylase (EC 4.1.1.88, malonate decarboxylase (without biotin), malonate decarboxylase, MDC) is an enzyme with systematic name malonate carboxy-lyase (biotin-independent). This enzyme catalyses the following chemical reaction

Biotin-dependent malonate decarboxylase (EC 4.1.1.89, malonate decarboxylase (with biotin), malonate decarboxylase) is an enzyme with systematic name malonate carboxy-lyase (biotin-dependent). This enzyme catalyses the following chemical reaction

Carboxybiotin decarboxylase (EC 7.2.4.1, MadB, carboxybiotin protein decarboxylase) is an enzyme with systematic name carboxybiotinyl-(protein) carboxy-lyase. This enzyme catalyses the following chemical reaction

Acetate—[acyl-carrier protein] ligase is an enzyme with systematic name acetate:(acyl-carrier-protein) ligase (AMP-forming). This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Ketoacyl synthase</span> Catalyst for a key step in fatty acid synthesis

Ketoacyl synthases (KSs) catalyze the condensation reaction of acyl-CoA or acyl-acyl ACP with malonyl-CoA to form 3-ketoacyl-CoA or with malonyl-ACP to form 3-ketoacyl-ACP. This reaction is a key step in the fatty acid synthesis cycle, as the resulting acyl chain is two carbon atoms longer than before. KSs exist as individual enzymes, as they do in type II fatty acid synthesis and type II polyketide synthesis, or as domains in large multidomain enzymes, such as type I fatty acid synthases (FASs) and polyketide synthases (PKSs). KSs are divided into five families: KS1, KS2, KS3, KS4, and KS5.

The Malonate:Na+ Symporter (MSS) Family (TC# 2.A.70) is a group of transport proteins belonging to the CPA superfamily. These proteins are composites with constituents ranging in size from 129 to 255 amino acyl residues (aas) and exhibiting 4 to 7 transmembrane segments (TMSs). A representative list of proteins belonging to the MSS family can be found in the Transporter Classification Database.

The Na+-transporting Carboxylic Acid Decarboxylase (NaT-DC) Family (TC# 3.B.1) is a family of porters that belong to the CPA superfamily. Members of this family have been characterized in both Gram-positive and Gram-negative bacteria. A representative list of proteins belonging to the NaT-DC family can be found in the Transporter Classification Database.

References

  1. Berg M, Hilbi H, Dimroth P (April 1997). "Sequence of a gene cluster from Malonomonas rubra encoding components of the malonate decarboxylase Na+ pump and evidence for their function". European Journal of Biochemistry. 245 (1): 103–15. doi: 10.1111/j.1432-1033.1997.00103.x . PMID   9128730.
  2. Micklefield J, Harris KJ, Gröger S, Mocek U, Hilbi H, Dimroth P, Floss HG (1995). "Stereochemical course of malonate decarboxylase in Malonomonas rubra has biotin decarboxylation with retention". J. Am. Chem. Soc. 117: 1153–1154. doi:10.1021/ja00108a042.
  3. Dimroth P, Hilbi H (July 1997). "Enzymic and genetic basis for bacterial growth on malonate". Molecular Microbiology. 25 (1): 3–10. doi: 10.1046/j.1365-2958.1997.4611824.x . PMID   11902724.