Pantetheine-phosphate adenylyltransferase

Last updated
pantetheine-phosphate adenylyltransferase
1vlh.png
Phosphopantetheine adenylyltransferase from Thermotoga maritima . 4'-Phosphopantetheine shown as spheres. PDB 1vlh
Identifiers
EC no. 2.7.7.3
CAS no. 9026-99-7
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 pantetheine-phosphate adenylyltransferase (EC 2.7.7.3) is an enzyme that catalyzes the chemical reaction

ATP + 4'-Phosphopantetheine diphosphate + 3'-dephospho-CoA

Thus, the two substrates of this enzyme are ATP and 4'-Phosphopantetheine, whereas its two products are diphosphate and 3'-dephospho-CoA.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:pantetheine-4'-phosphate adenylyltransferase. Other names in common use include dephospho-CoA pyrophosphorylase, pantetheine phosphate adenylyltransferase, dephospho-coenzyme A pyrophosphorylase, and 3'-dephospho-CoA pyrophosphorylase. This enzyme participates in pantothenate and coa biosynthesis.

Structural studies

As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1B6T, 1GN8, 1H1T, 1O6B, 1OD6, 1QJC, 1TFU, and 1VLH.

Related Research Articles

<span class="mw-page-title-main">Coenzyme A</span> Coenzyme, notable for its synthesis and oxidation role

Coenzyme A (CoA, SHCoA, CoASH) is a coenzyme, notable for its role in the synthesis and oxidation of fatty acids, and the oxidation of pyruvate in the citric acid cycle. All genomes sequenced to date encode enzymes that use coenzyme A as a substrate, and around 4% of cellular enzymes use it (or a thioester) as a substrate. In humans, CoA biosynthesis requires cysteine, pantothenate (vitamin B5), and adenosine triphosphate (ATP).

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

Pantetheine is the cysteamine amide analog of pantothenic acid (vitamin B5). The dimer of this compound, pantethine is more commonly known, and is considered to be the most potent form of vitamin B5. Pantetheine is an intermediate in the catabolism of coenzyme A by the body.

The crotonase family comprises mechanistically diverse proteins that share a conserved trimeric quaternary structure, the core of which consists of 4 turns of a (beta/beta/alpha)n superhelix.

<span class="mw-page-title-main">UDP-glucose 4-epimerase</span> Class of enzymes

The enzyme UDP-glucose 4-epimerase, also known as UDP-galactose 4-epimerase or GALE, is a homodimeric epimerase found in bacterial, fungal, plant, and mammalian cells. This enzyme performs the final step in the Leloir pathway of galactose metabolism, catalyzing the reversible conversion of UDP-galactose to UDP-glucose. GALE tightly binds nicotinamide adenine dinucleotide (NAD+), a co-factor required for catalytic activity.

<span class="mw-page-title-main">Dihydrofolate synthase</span> Class of enzymes

In enzymology, a dihydrofolate synthase is an enzyme that catalyzes the chemical reaction

In enzymology, a pantoate—β-alanine ligase is an enzyme that catalyzes the chemical reaction

In enzymology, a phosphopantothenate—cysteine ligase also known as phosphopantothenoylcysteine synthetase (PPCS) is an enzyme that catalyzes the chemical reaction which constitutes the second of five steps involved in the conversion of pantothenate to Coenzyme A. The reaction is:

In enzymology, a serine—tRNA ligase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Succinate—CoA ligase (ADP-forming)</span>

In enzymology, a succinate-CoA ligase (ADP-forming) is an enzyme that catalyzes the chemical reaction

In enzymology, a tetrahydrofolate synthase is an enzyme that catalyzes the chemical reaction

The enzyme [acyl-carrier-protein] phosphodiesterase (EC 3.1.4.14) catalyzes the reaction

<span class="mw-page-title-main">ATP phosphoribosyltransferase</span> Class of enzymes

In enzymology, an ATP phosphoribosyltransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Nicotinate phosphoribosyltransferase</span>

In enzymology, a nicotinate phosphoribosyltransferase (EC 6.3.4.21) is an enzyme that catalyzes the chemical reaction

In enzymology, a 3-deoxy-manno-octulosonate cytidylyltransferase is an enzyme that catalyzes the chemical reaction

Choline-phosphate cytidylyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a dephospho-CoA kinase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Glucose-1-phosphate adenylyltransferase</span>

In enzymology, a glucose-1-phosphate adenylyltransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Nicotinamide-nucleotide adenylyltransferase</span>

In enzymology, nicotinamide-nucleotide adenylyltransferase (NMNAT) (EC 2.7.7.1) are enzymes that catalyzes the chemical reaction

In enzymology, a nicotinate-nucleotide adenylyltransferase (EC 2.7.7.18) is an enzyme that catalyzes the chemical reaction

CCA tRNA nucleotidyltransferase is an enzyme with systematic name CTP,CTP,ATP:tRNA cytidylyl,cytidylyl,adenylyltransferase. This enzyme catalyses the following chemical reaction

References