L-amino-acid oxidase: Difference between revisions

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{{enzyme
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| Name = L-methionine (R)-S-oxide reductase
| EC_number = 1.8.4.14
| CAS_number =
| IUBMB_EC_number = 1/8/4/14
| GO_code =
| image =
| width =
| caption =
}}
{{Orphan|date=February 2009}}
In [[enzymology]], a '''L-methionine (R)-S-oxide reductase''' ({{EC number|1.8.4.14}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
 
:L-methionine + thioredoxin disulfide + H<sub>2</sub>O <math>\rightleftharpoons</math> L-methionine (R)-S-oxide + thioredoxin
 
The 3 [[substrate (biochemistry)|substrates]] of this enzyme are [[L-methionine]], [[thioredoxin disulfide]], and [[water|H<sub>2</sub>O]], whereas its two [[product (chemistry)|products]] are [[L-methionine (R)-S-oxide]] and [[thioredoxin]].
 
This enzyme belongs to the family of [[oxidoreductase]]s, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is '''L-methionine:thioredoxin-disulfide S-oxidoreductase [L-methionine (R)-S-oxide-forming]'''. Other names in common use include '''fRMsr''', '''FRMsr''', '''free met-R-(o) reductase''', and '''free-methionine (R)-S-oxide reductase'''.  This enzyme participates in [[methionine metabolism]]. 
 
==References==
{{reflist|1}}
* {{cite journal | author = Etienne F, Spector D, Brot N, Weissbach H | date = 2003 | title = A methionine sulfoxide reductase in Escherichia coli that reduces the R enantiomer of methionine sulfoxide | journal = Biochem. Biophys. Res. Commun.  | volume = 300 | pages = 378&ndash;82  | pmid = 12504094 | doi = 10.1016/S0006-291X(02)02870-X | issue = 2 }}
 
{{1.8-enzyme-stub}}
 
[[Category:EC 1.8.4]]
[[Category:Enzymes of unknown structure]]

Latest revision as of 12:19, 27 October 2014

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