“Arginine deiminase”的意思、由来-开放百科全书

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Arginine deiminase

释义

Structural studies
References

{{enzyme
| Name = arginine deiminase
| EC_number = 3.5.3.6
| CAS_number = 9027-98-9
| IUBMB_EC_number = 3/5/3/6
| GO_code = 0016990
| image =
| width =
| caption =
}}

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

L-arginine + H₂O L-citrulline + NH₃

Thus, the two substrates of this enzyme are L-arginine and H₂O, whereas its two products are L-citrulline and NH₃.

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 L-arginine iminohydrolase. Other names in common use include arginine dihydrolase, citrulline iminase, and L-arginine deiminase. This enzyme participates in arginine and proline metabolism. This enzyme is widely expressed in bacteria, including streptococcus and actinomyces. The bacterial arginine deiminase expression could be regulated by various environmental factors.

Recently, a new enzyme that catalyzes the chemical reaction

L-arginine + 2H₂O L-ornithine + 2NH₃ + CO₂ was identified in cyanobacteria^[1] which should be named as arginine dihydrolase.

Structural studies

As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1LXY}}, {{PDB link|1RXX}}, {{PDB link|1S9R}}, {{PDB link|2A9G}}, {{PDB link|2AAF}}, {{PDB link|2ABR}}, and {{PDB link|2ACI}}.

References

{{cite journal | vauthors = OGINSKY EL, GEHRIG RF | year = 1952 | title = The arginine dihydrolase system of Streptococcus faecalis. II Properties of arginine desimidase | journal = J. Biol. Chem. | volume = 198 | pages = 799–805 | pmid = 12999797 | issue = 2 }}
{{cite journal | vauthors = LIU Y, BURNE RA | year = 2009 | title = Multiple two-component systems modulate alkali generation in Streptococcus gordonii in response to environmental stresses | journal = J. Bacteriol. | volume = 191 | pages = 7353–7362 | pmid = 19783634 | doi=10.1128/JB.01053-09 | pmc=2786566}}
{{cite journal | vauthors = PETRAK B, SULLIAN L , RETARN S | year = 1957 | title = Behavior of purified arginine deiminase from S. faecalis | journal = Arch. Biochem. Biophys. | volume = 69 | pages = 186–197 | doi = 10.1016/0003-9861(57)90485-X | pmid=13445192}}
{{cite journal | author = RATNER S | year = 1954 | title = Urea synthesis and metabolism of arginine and citrulline | journal = Adv. Enzymol. Relat. Subj. Biochem. | volume = 15 | pages = 319–87 | pmid = 13158183 }}
{{cite journal | vauthors = LIU Y, BURNE RA | year = 2008 | title = Environmental and growth phase regulation of the Streptococcus gordonii arginine deiminase genes | journal = Appl Environ Microbiol | volume = 74| pages = 5023–5030 |doi = 10.1128/AEM.00556-08| pmid = 18552185 | issue = 16 | pmc=2519279}}

{{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 known structure

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