Long-chain acyl-(acyl-carrier-protein) reductase

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Long-chain acyl-(acyl-carrier-protein) reductase
Identifiers
EC no. 1.2.1.80
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NCBI proteins

Long-chain acyl-(acyl-carrier-protein) reductase (EC 1.2.1.80, long-chain acyl-[acp] reductase, fatty acyl-[acyl-carrier-protein] reductase, acyl-[acp] reductase) is an enzyme with systematic name long-chain-aldehyde:NAD(P)+ oxidoreductase (acyl-(acyl-carrier protein)-forming). [1] This enzyme catalyses the following chemical reaction

a long-chain aldehyde + acyl-carrier protein + NAD(P)+ a long-chain acyl-[acyl-carrier protein] + NAD(P)H + H+

This enzyme catalyses the reaction in the opposite direction.

Related Research Articles

A dehydrogenase is an enzyme belonging to the group of oxidoreductases that oxidizes a substrate by reducing an electron acceptor, usually NAD+/NADP+ or a flavin coenzyme such as FAD or FMN. Like all catalysts, they catalyze reverse as well as forward reactions, and in some cases this has physiological significance: for example, alcohol dehydrogenase catalyzes the oxidation of ethanol to acetaldehyde in animals, but in yeast it catalyzes the production of ethanol from acetaldehyde.

<span class="mw-page-title-main">Enoyl-acyl carrier protein reductase</span> InterPro Family

Enoyl-acyl carrier protein reductase, is a key enzyme of the type II fatty acid synthesis (FAS) system. ENR is an attractive target for narrow-spectrum antibacterial drug discovery because of its essential role in metabolism and its sequence conservation across many bacterial species. In addition, the bacterial ENR sequence and structural organization are distinctly different from those of mammalian fatty acid biosynthesis enzymes.

<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">3-oxoacyl-(acyl-carrier-protein) reductase</span> Enzyme

In enzymology, a 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) is an enzyme that catalyzes the chemical reaction

In enzymology, a 3-oxoacyl-[acyl-carrier-protein] reductase (NADH) (EC 1.1.1.212) is an enzyme that catalyzes the chemical reaction

In enzymology, an enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) (EC 1.3.1.39) is an enzyme that catalyzes the chemical reaction

In enzymology, an enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) (EC 1.3.1.10) is an enzyme that catalyzes the chemical reaction

In enzymology, a long-chain-fatty-acyl-CoA reductase (EC 1.2.1.50) is an enzyme that catalyzes the chemical reaction

In enzymology, a mycothiol-dependent formaldehyde dehydrogenase (EC 1.1.1.306) is an enzyme that catalyzes the chemical reaction

In enzymology, a long-chain-fatty-acid—[acyl-carrier-protein] ligase 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">Short-chain acyl-CoA dehydrogenase</span>

Short-chain acyl-CoA dehydrogenase is an enzyme with systematic name short-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase. This enzyme catalyses the following chemical reaction

Malonyl-S-ACP:biotin-protein carboxyltransferase is an enzyme with systematic name malonyl-(acyl-carrier protein):biotinyl-(protein) carboxytransferase. This enzyme catalyses the following chemical reaction

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

UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase is an enzyme with systematic name (3R)-3-hydroxymyristoyl-(acyl-carrier protein):UDP-3-O-( -3-hydroxymyristoyl)-alpha-D-glucosamine N-acetyltransferase. 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

3-hydroxydecanoyl-(acyl-carrier-protein) dehydratase (EC 4.2.1.60, D-3-hydroxydecanoyl-[acyl-carrier protein] dehydratase, 3-hydroxydecanoyl-acyl carrier protein dehydrase, 3-hydroxydecanoyl-acyl carrier protein dehydratase, β-hydroxydecanoyl thioester dehydrase, β-hydroxydecanoate dehydrase, beta-hydroxydecanoyl thiol ester dehydrase, FabA, β-hydroxyacyl-acyl carrier protein dehydratase, HDDase, β-hydroxyacyl-ACP dehydrase, (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] hydro-lyase) is an enzyme with systematic name (3R)-3-hydroxydecanoyl-(acyl-carrier protein) hydro-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.

<span class="mw-page-title-main">Aldehyde deformylating oxygenase</span> Enzyme family

Aldehyde deformylating oxygenases (ADO) (EC 4.1.99.5) are a family of enzymes which catalyze the oxygenation of medium and long chain aldehydes to alkanes via the removal of a carbonyl group as formate.

References

  1. Schirmer A, Rude MA, Li X, Popova E, del Cardayre SB (July 2010). "Microbial biosynthesis of alkanes". Science. 329 (5991): 559–62. doi:10.1126/science.1187936. PMID   20671186.