“N-succinylarginine dihydrolase”的意思、由来-开放百科全书

词条

N-succinylarginine dihydrolase

释义

References

{{enzyme
| Name = N-succinylarginine dihydrolase
| EC_number = 3.5.3.23
| CAS_number =
| IUBMB_EC_number = 3/5/3/23
| GO_code = 0009015
| image =
| width =
| caption =
}}

In enzymology, a N-succinylarginine dihydrolase ({{EC number|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.

References

{{cite journal |vauthors=Schneider BL, Kiupakis AK, Reitzer LJ | date = 1998 | title = Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli | journal = J. Bacteriol. | volume = 180 | pages = 4278–86 | pmid = 9696779 | issue = 16 | pmc = 107427 }}
{{cite journal | author = M | date = 2005 | title = Crystal structure of N-succinylarginine dihydrolase AstB, bound to substrate and product, an enzyme from the arginine catabolic pathway of Escherichia coli | journal = J. Biol. Chem. | volume = 280 | pages = 15800–8 | pmid = 15703173 | doi = 10.1074/jbc.M413833200 | last2 = Schrag | first2 = JD | last3 = Li | first3 = Y | last4 = Schneider | first4 = BL | last5 = Reitzer | first5 = L | last6 = Matte | first6 = A | last7 = Cygler | first7 = M | issue = 16 }}
{{cite journal |vauthors=Vander Wauven C, Stalon V | date = 1985 | title = Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia | journal = J. Bacteriol. | volume = 164 | pages = 882–6 | pmid = 2865249 | issue = 2 | pmc = 214334 }}
{{cite journal |vauthors=Cunin R, Glansdorff N, Pierard A, Stalon V | date = 1986 | title = Biosynthesis and metabolism of arginine in bacteria | journal = Microbiol. Rev. | volume = 50 | pages = 314–52 | pmid = 3534538 | issue = 3 | pmc = 373073 }}
{{cite journal | author = Itoh Y | date = 1997 | title = Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa | journal = J. Bacteriol. | volume = 179 | pages = 7280–90 | pmid = 9393691 | issue = 23 | pmc = 179677 }}

{{Carbon-nitrogen non-peptide hydrolases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{3.5-enzyme-stub}}

2 : EC 3.5.3|Enzymes of unknown structure

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