Glutaryl-CoA

Last updated
Glutaryl-CoA
Glutaryl coenzyme A.svg
Names
IUPAC name
5-[(2-{3-[(2R)-4-{[1,3-Dihydroxy-1,3-dioxo-3-(3′-O-phosphonoadenosin-5′-O-yl)-1λ5,3λ5-diphosphoxan-1-yl]oxy}-3,3-dimethylbutanamido]propanamido}ethyl)sulfanyl]-5-oxopentanoic acid
Systematic IUPAC name
(9R)-1-[(2R,3S,4R,5R)-5-(6-Amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5,10,14,19-pentaoxo-2,4,6-trioxa-18-thia-11,15-diaza-3λ5,5λ5-diphosphatricosan-23-oic acid
Identifiers
3D model (JSmol)
ChemSpider
MeSH Glutaryl-coenzyme+A
PubChem CID
  • InChI=1S/C26H42N7O19P3S/c1-26(2,21(39)24(40)29-7-6-15(34)28-8-9-56-17(37)5-3-4-16(35)36)11-49-55(46,47)52-54(44,45)48-10-14-20(51-53(41,42)43)19(38)25(50-14)33-13-32-18-22(27)30-12-31-23(18)33/h12-14,19-21,25,38-39H,3-11H2,1-2H3,(H,28,34)(H,29,40)(H,35,36)(H,44,45)(H,46,47)(H2,27,30,31)(H2,41,42,43)/t14-,19-,20-,21+,25-/m1/s1 X mark.svgN
    Key: SYKWLIJQEHRDNH-CKRMAKSASA-N X mark.svgN
  • InChI=1/C26H42N7O19P3S/c1-26(2,21(39)24(40)29-7-6-15(34)28-8-9-56-17(37)5-3-4-16(35)36)11-49-55(46,47)52-54(44,45)48-10-14-20(51-53(41,42)43)19(38)25(50-14)33-13-32-18-22(27)30-12-31-23(18)33/h12-14,19-21,25,38-39H,3-11H2,1-2H3,(H,28,34)(H,29,40)(H,35,36)(H,44,45)(H,46,47)(H2,27,30,31)(H2,41,42,43)/t14-,19-,20-,21+,25-/m1/s1
    Key: SYKWLIJQEHRDNH-CKRMAKSABC
  • O=C(O)CCCC(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)COP(=O)(O)OP(=O)(O)OC[C@H]3O[C@@H](n2cnc1c(ncnc12)N)[C@H](O)[C@@H]3OP(=O)(O)O
Properties
C26H42N7O19P3S
Molar mass 881.635 g/mol
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
X mark.svgN  verify  (what is  Yes check.svgYX mark.svgN ?)

Glutaryl-coenzyme A is an intermediate in the metabolism of lysine and tryptophan. [1]

See also

Related Research Articles

<span class="mw-page-title-main">Lysine</span> Amino acid

Lysine (symbol Lys or K) is an α-amino acid that is a precursor to many proteins. It contains an α-amino group (which is in the protonated −NH+
3 form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO− form under biological conditions), and a side chain lysyl ((CH2)4NH2), classifying it as a basic, charged (at physiological pH), aliphatic amino acid. It is encoded by the codons AAA and AAG. Like almost all other amino acids, the α-carbon is chiral and lysine may refer to either enantiomer or a racemic mixture of both. For the purpose of this article, lysine will refer to the biologically active enantiomer L-lysine, where the α-carbon is in the S configuration.

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

Acetyl-CoA is a molecule that participates in many biochemical reactions in protein, carbohydrate and lipid metabolism. Its main function is to deliver the acetyl group to the citric acid cycle to be oxidized for energy production. Coenzyme A consists of a β-mercaptoethylamine group linked to the vitamin pantothenic acid (B5) through an amide linkage and 3'-phosphorylated ADP. The acetyl group of acetyl-CoA is linked to the sulfhydryl substituent of the β-mercaptoethylamine group. This thioester linkage is a "high energy" bond, which is particularly reactive. Hydrolysis of the thioester bond is exergonic (−31.5 kJ/mol).

<span class="mw-page-title-main">Flavin adenine dinucleotide</span> Redox-active coenzyme

In biochemistry, flavin adenine dinucleotide (FAD) is a redox-active coenzyme associated with various proteins, which is involved with several enzymatic reactions in metabolism. A flavoprotein is a protein that contains a flavin group, which may be in the form of FAD or flavin mononucleotide (FMN). Many flavoproteins are known: components of the succinate dehydrogenase complex, α-ketoglutarate dehydrogenase, and a component of the pyruvate dehydrogenase complex.

Glutaric acidemia type 1 (GA1) is an inherited disorder in which the body is unable to completely break down the amino acids lysine, hydroxylysine and tryptophan. Excessive levels of their intermediate breakdown products can accumulate and cause damage to the brain, but particularly the basal ganglia, which are regions that help regulate movement. GA1 causes secondary carnitine deficiency, as glutaric acid, like other organic acids, is detoxified by carnitine. Mental retardation may occur.

<span class="mw-page-title-main">Glutaryl-CoA dehydrogenase</span> Protein-coding gene in the species Homo sapiens

Glutaryl-CoA dehydrogenase (GCDH) is an enzyme encoded by the GCDH gene on chromosome 19. The protein belongs to the acyl-CoA dehydrogenase family (ACD). It catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor. The enzyme exists in the mitochondrial matrix as a homotetramer of 45-kD subunits. Mutations in this gene result in the metabolic disorder glutaric aciduria type 1, which is also known as glutaric acidemia type I. Alternative splicing of this gene results in multiple transcript variants.

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

Crotonyl-coenzyme A is an intermediate in the fermentation of butyric acid, and in the metabolism of lysine and tryptophan. It is important in the metabolism of fatty acids and amino acids.

<span class="mw-page-title-main">3-hydroxyacyl-CoA dehydrogenase</span> Enzyme

In enzymology, a 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">3-Hydroxybutyryl-CoA dehydrogenase</span>

In enzymology, a 3-hydroxybutyryl-CoA dehydrogenase (EC 1.1.1.157) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Saccharopine dehydrogenase (NAD+, L-lysine-forming)</span>

In enzymology, a saccharopine dehydrogenase (NAD+, L-lysine-forming) (EC 1.5.1.7) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Saccharopine dehydrogenase (NADP+, L-glutamate-forming)</span>

In enzymology, a saccharopine dehydrogenase (NADP+, L-glutamate-forming) (EC 1.5.1.10) is an enzyme that catalyzes the chemical reaction

In enzymology, a 3-oxoacid CoA-transferase is an enzyme that catalyzes the chemical reaction

The enzyme 3-hydroxy-3-isohexenylglutaryl-CoA lyase catalyzes the chemical reaction

In enzymology, a glutarate—CoA ligase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Alpha-aminoadipic semialdehyde synthase</span> Protein-coding gene in the species Homo sapiens

Alpha-aminoadipic semialdehyde synthase is an enzyme encoded by the AASS gene in humans and is involved in their major lysine degradation pathway. It is similar to the separate enzymes coded for by the LYS1 and LYS9 genes in yeast, and related to, although not similar in structure, the bifunctional enzyme found in plants. In humans, mutations in the AASS gene, and the corresponding alpha-aminoadipic semialdehyde synthase enzyme are associated with familial hyperlysinemia. This condition is inherited in an autosomal recessive pattern and is not considered a particularly negative condition, thus making it a rare disease.

Glutaconyl-CoA is an intermediate in the metabolism of lysine. It is an organic compound containing a coenzyme substructure, which classifies it as a fatty ester lipid molecule. Being a lipid makes the molecule hydrophobic, which makes it insoluble in water. The molecule has a molecular formula of C26H40N7O19P3S, and a molecular weight 879.62 grams per mole.

Glutaryl-CoA dehydrogenase (non-decarboxylating) is an enzyme with systematic name glutaryl-CoA:acceptor 2,3-oxidoreductase (non-decarboxylating). This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">DHTKD1</span> Protein-coding gene in the species Homo sapiens

Dehydrogenase E1 and transketolase domain containing 1 is a protein that in humans is encoded by the DHTKD1 gene. This gene encodes a component of a mitochondrial 2-oxoglutarate-dehydrogenase-complex-like protein involved in the degradation pathways of several amino acids, including lysine. Mutations in this gene are associated with 2-aminoadipic 2-oxoadipic aciduria and Charcot-Marie-Tooth Disease Type 2Q.

References

  1. ↑ Rao KS, Albro M, Dwyer TM, Frerman FE (Dec 2006). "Kinetic mechanism of glutaryl-CoA dehydrogenase". Biochemistry. 45 (51): 15853–61. doi:10.1021/bi0609016. PMID   17176108.


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