N-succinylarginine dihydrolase

Last updated
N-succinylarginine dihydrolase
Identifiers
EC no. 3.5.3.23
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 N-succinylarginine dihydrolase (EC 3.5.3.23) is an enzyme that catalyzes the chemical reaction

N2-succinyl-L-arginine + 2 H2O N2-succinyl-L-ornithine + 2 NH3 + CO2

Thus, the two substrates of this enzyme are N2-succinyl-L-arginine and H2O, whereas its 3 products are N2-succinyl-L-ornithine, NH3, and CO2.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is N2-succinyl-L-arginine iminohydrolase (decarboxylating). Other names in common use include N2-succinylarginine dihydrolase, arginine succinylhydrolase, SADH, AruB, AstB, and 2-N-succinyl-L-arginine iminohydrolase (decarboxylating). This enzyme participates in arginine and proline metabolism.

Related Research Articles

A bradytroph is a strain of an organism that exhibits slow growth in the absence of an external source of a particular metabolite. This is usually due to a defect in an enzyme required in the metabolic pathway producing this chemical. Such defects are the result of mutations in the genes encoding these enzymes. As the organism can still produce small amounts of the chemical, the mutation is not lethal. In these bradytroph strains, rapid growth occurs when the chemical is present in the cell's growth media and the missing metabolite can be transported into the cell from the external environment. A bradytroph may also be referred to as a "leaky auxotroph".

<span class="mw-page-title-main">6-Phosphogluconate dehydrogenase</span> Class of enzymes

6-Phosphogluconate dehydrogenase (6PGD) is an enzyme in the pentose phosphate pathway. It forms ribulose 5-phosphate from 6-phosphogluconate:

In enzymology, a succinylglutamate-semialdehyde dehydrogenase (EC 1.2.1.71) is an enzyme that catalyzes the chemical reaction

In enzymology, a 5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase (EC 1.2.1.60) is an enzyme that catalyzes the chemical reaction

In enzymology, an aminobutyraldehyde dehydrogenase (EC 1.2.1.19) is an enzyme that catalyzes the chemical reaction

In enzymology, an acetate CoA-transferase is an enzyme that catalyzes the chemical reaction

In enzymology, a succinyl-CoA:(R)-benzylsuccinate CoA-transferase is an enzyme that catalyzes the chemical reaction

In enzymology, an acetylornithine deacetylase (EC 3.5.1.16) is an enzyme that catalyzes the chemical reaction

In enzymology, an arginine deiminase (EC 3.5.3.6) is an enzyme that catalyzes the chemical reaction

In enzymology, a succinylglutamate desuccinylase (EC 3.5.1.96) is an enzyme that catalyzes the chemical reaction

In enzymology, a 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase (EC 2.3.1.117) is an enzyme that catalyzes the chemical reaction

In enzymology, an arginine N-succinyltransferase (EC 2.3.1.109) is an enzyme that catalyzes the chemical reaction

In enzymology, an acetylornithine transaminase (EC 2.6.1.11) is an enzyme that catalyzes the chemical reaction

In enzymology, an arginine-pyruvate transaminase is an enzyme that catalyzes the chemical reaction

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

In enzymology, a succinylornithine transaminase (EC 2.6.1.81) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">ATCase/OTCase family</span>

In molecular biology, the ATCase/OTCase family is a protein family which contains two related enzymes: aspartate carbamoyltransferase EC 2.1.3.2 and ornithine carbamoyltransferase EC 2.1.3.3. It has been shown that these enzymes are evolutionary related. The predicted secondary structure of both enzymes is similar and there are some regions of sequence similarities. One of these regions includes three residues which have been shown, by crystallographic studies to be implicated in binding the phosphoryl group of carbamoyl phosphate and may also play a role in trimerisation of the molecules. The N-terminal domain is the carbamoyl phosphate binding domain. The C-terminal domain is an aspartate/ornithine-binding domain.

3-(3-hydroxyphenyl)propanoate hydroxylase (EC 1.14.13.127, mhpA (gene)) is an enzyme with systematic name 3-(3-hydroxyphenyl)propanoate,NADH:oxygen oxidoreductase (2-hydroxylating). This enzyme catalyses the following chemical reaction

Phenylacetyl-CoA 1,2-epoxidase (EC 1.14.13.149, ring 1,2-phenylacetyl-CoA epoxidase, phenylacetyl-CoA monooxygenase, PaaAC, PaaABC(D)E) is an enzyme with systematic name phenylacetyl-CoA:oxygen oxidoreductase (1,2-epoxidizing). This enzyme catalyses the following chemical reaction

3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase (EC 1.17.1.7, paaZ (gene)) is an enzyme with systematic name 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction

Oxepin-CoA hydrolase (EC 3.7.1.16, paaZ (gene)) is an enzyme with systematic name 2-oxepin-2(3H)-ylideneacetyl-CoA hydrolyase. This enzyme catalyses the following chemical reaction

References