4-hydroxybenzoate polyprenyltransferase

Last updated
4-hydroxybenzoate polyprenyltransferase
Identifiers
EC no. 2.5.1.39
CAS no. 9030-77-7
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

In enzymology, a 4-hydroxybenzoate polyprenyltransferase (EC 2.5.1.39) is an enzyme that catalyzes the chemical reaction

a polyprenyl diphosphate + 4-hydroxybenzoate diphosphate + a 4-hydroxy-3-polyprenylbenzoate

Thus, the two substrates of this enzyme are a polyprenyl diphosphate and 4-hydroxybenzoate, whereas its two products are diphosphate and 4-hydroxy-3-polyprenylbenzoate.

This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. This enzyme participates in ubiquinone biosynthesis. [1]

Nomenclature

The systematic name of this enzyme class is polyprenyl-diphosphate:4-hydroxybenzoate polyprenyltransferase. Other names in common use include:

Related Research Articles

Juvenile hormones (JHs) are a group of acyclic sesquiterpenoids that regulate many aspects of insect physiology. The first discovery of a JH was by Vincent Wigglesworth. JHs regulate development, reproduction, diapause, and polyphenisms. The chemical formula for juvenile hormone is .

Dolichol refers to any of a group of long-chain mostly unsaturated organic compounds that are made up of varying numbers of isoprene units terminating in an α-saturated isoprenoid group, containing an alcohol functional group.

4-Hydroxybenzoic acid, also known as p-hydroxybenzoic acid (PHBA), is a monohydroxybenzoic acid, a phenolic derivative of benzoic acid. It is a white crystalline solid that is slightly soluble in water and chloroform but more soluble in polar organic solvents such as alcohols and acetone. 4-Hydroxybenzoic acid is primarily known as the basis for the preparation of its esters, known as parabens, which are used as preservatives in cosmetics and some ophthalmic solutions. It is isomeric with 2-hydroxybenzoic acid, known as salicylic acid, a precursor to aspirin, and with 3-hydroxybenzoic acid.

In enzymology, a 3-demethylubiquinone-9 3-O-methyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a hexaprenyldihydroxybenzoate methyltransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Chorismate lyase</span>

The enzyme chorismate lyase catalyzes the first step in ubiquinone biosynthesis, the removal of pyruvate from chorismate, to yield 4-hydroxybenzoate in Escherichia coli and other Gram-negative bacteria. It belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is chorismate pyruvate-lyase (4-hydroxybenzoate-forming). Other names in common use include CL, CPL, and UbiC.

<span class="mw-page-title-main">Diphosphomevalonate decarboxylase</span> InterPro Family

Diphosphomevalonate decarboxylase (EC 4.1.1.33), most commonly referred to in scientific literature as mevalonate diphosphate decarboxylase, is an enzyme that catalyzes the chemical reaction

In enzymology, a rubber cis-polyprenylcistransferase (EC 2.5.1.20) is an enzyme that catalyzes the chemical reaction

In enzymology, a tryptophan dimethylallyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a dolichyl-phosphate beta-D-mannosyltransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase</span> Enzyme

In enzymology, a 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">PDSS1</span> Protein-coding gene in the species Homo sapiens

Decaprenyl-diphosphate synthase subunit 1 is an enzyme that in humans is encoded by the PDSS1 gene.

<span class="mw-page-title-main">COQ2</span> Protein-coding gene in the species Homo sapiens

Para-hydroxybenzoate—polyprenyltransferase, mitochondrial is an enzyme that in humans is encoded by the COQ2 gene.

<span class="mw-page-title-main">UbiD protein domain</span>

In molecular biology this protein domain, refers to UbiD, which is found in prokaryotes, archaea and fungi, with two members in Archaeoglobus fulgidus. They are related to UbiD, a 3-octaprenyl-4-hydroxybenzoate carboxy-lyase from Escherichia coli that is involved in ubiquinone biosynthesis. The member from Helicobacter pylori has a C-terminal extension of just over 100 residues that is shared, in part, by the Aquifex aeolicus homologue.

1-4-dihydroxy-2-napthoate (DHNA) polyprenyltransferase (EC 2.5.1.74)is an enzyme that catalyzes the chemical reaction: all-trans-nonaprenyl diphosphate + 1-4-dihydroxy-2-napthoate + H+ demethylmenaquinol-9 + diphosphate + carbon dioxide

All-trans-nonaprenyl-diphosphate synthase is an enzyme with systematic name geranyl-diphosphate:isopentenyl-diphosphate transtransferase . This enzyme catalyses the following chemical reaction

Ditrans,polycis-polyprenyl diphosphate synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate cistransferase . This enzyme catalyses the following chemical reaction

4-hydroxybenzoate geranyltransferase is an enzyme with systematic name geranyl-diphosphate:4-hydroxybenzoate 3-geranyltransferase. This enzyme catalyses the following chemical reaction

<i>Lithospermum erythrorhizon</i> Species of flowering plant in the borage family Boraginaceae

Lithospermum erythrorhizon, commonly called purple gromwell, red stoneroot, red gromwell, red-root gromwell and redroot lithospermum, is a plant species in the family Boraginaceae. It is called zǐcǎo (紫草) in Chinese, jichi (지치) in Korean, and murasaki in Japanese.

Rhodoquinone Chemical compound

Rhodoquinone (RQ) is a modified ubiquinone-like molecule that is an important cofactor used in anaerobic energy metabolism by many organisms. Recently, it has gained attention as a potential anthelmintic drug target due to the fact that parasitic hosts do not synthesize or use this cofactor. Because this cofactor is used in low oxygen environments, many helminth-like organisms have adapted to survive host environments such as the areas within the gastrointestinal tracks.

References

  1. Melzer M, Heide L (1994-04-14). "Characterization of polyprenyldiphosphate: 4-hydroxybenzoate polyprenyltransferase from Escherichia coli". Biochim Biophys Acta. 1212 (1): 93–102. doi:10.1016/0005-2760(94)90193-7. PMID   8155731.