ADP deaminase

Last updated
ADP deaminase
Identifiers
EC no. 3.5.4.7
CAS no. 9027-79-6
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, an ADP deaminase (EC 3.5.4.7) is an enzyme that catalyzes the chemical reaction

ADP + H2O IDP + NH3

Thus, the two substrates of this enzyme are ADP and H2O, whereas its two products are IDP and NH3.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is ADP aminohydrolase. Other names in common use include adenosine diphosphate deaminase, and adenosinepyrophosphate deaminase.

Related Research Articles

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

The enzyme aspartate ammonia-lyase (EC 4.3.1.1) catalyzes the chemical reaction

<span class="mw-page-title-main">L-serine ammonia-lyase</span>

The enzyme L-serine ammonia-lyase (EC 4.3.1.17) catalyzes the chemical reaction

In enzymology, a 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) is an enzyme that catalyzes the chemical reaction

In enzymology, 2-aminomuconate deaminase (EC 3.5.99.5) (also known as amnd) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Adenine deaminase</span> InterPro Family

In enzymology, an adenine deaminase (EC 3.5.4.2) is an enzyme that catalyzes the chemical reaction

In enzymology, an adenosine-phosphate deaminase (EC 3.5.4.17) is an enzyme that catalyzes the chemical reaction

In enzymology, an ATP deaminase (EC 3.5.4.18) is an enzyme that catalyzes the chemical reaction

In enzymology, a creatinine deaminase (EC 3.5.4.21) is an enzyme that catalyzes the chemical reaction

In enzymology, a cytosine deaminase (EC 3.5.4.1) is an enzyme that catalyzes the chemical reaction

In enzymology, a dCTP deaminase (EC 3.5.4.13) is an enzyme that catalyzes the chemical reaction

In enzymology, a dCTP deaminase (dUMP-forming) (EC 3.5.4.30) is an enzyme that catalyzes the chemical reaction

In enzymology, a deoxycytidine deaminase (EC 3.5.4.5) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Glucosamine-6-phosphate deaminase</span>

In enzymology, a glucosamine-6-phosphate deaminase (EC 3.5.99.6) is an enzyme that catalyzes the chemical reaction

In enzymology, a guanosine deaminase (EC 3.5.4.15) is an enzyme that catalyzes the chemical reaction

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

In enzymology, a nicotinamidase (EC 3.5.1.19) is an enzyme that catalyzes the chemical reaction

In enzymology, a pterin deaminase (EC 3.5.4.11) is an enzyme that catalyzes the chemical reaction

In enzymology, a S-adenosylhomocysteine deaminase (EC 3.5.4.28) is an enzyme that catalyzes the chemical reaction

In enzymology, a sepiapterin deaminase (EC 3.5.4.24) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Starch synthase</span>

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

<span class="mw-page-title-main">Purine nucleotide cycle</span>

The Purine Nucleotide Cycle is a metabolic pathway in protein metabolism requiring the amino acids aspartate and glutamate. The cycle is used to regulate the levels of adenine nucleotides, in which ammonia and fumarate are generated. AMP coverts into IMP and the byproduct ammonia. IMP converts to S-AMP (adenylosuccinate), which then coverts to AMP and the byproduct fumarate. The fumarate goes on to produce ATP (energy) via oxidative phosphorylation as it enters the Krebs cycle and then the electron transport chain. Lowenstein first described this pathway and outlined its importance in processes including amino acid catabolism and regulation of flux through glycolysis and the Krebs cycle.

References


    This page is based on this Wikipedia article
    Text is available under the CC BY-SA 4.0 license; additional terms may apply.
    Images, videos and audio are available under their respective licenses.