Document Detail


Atomic Resolution Structure of an N(5) Flavin Adduct in D-Arginine Dehydrogenase.
MedLine Citation:
PMID:  21707047     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
D-Arginine dehydrogenase (DADH) catalyzes the flavin-dependent oxidative deamination of D-arginine and other D-amino acids to the corresponding imino acids. The 1.07 Å atomic resolution structure of DADH crystallized with D-leucine unexpectedly revealed a covalent flavin N(5) adduct, instead of the expected iminoleucine product in the active site. This acyl adduct has been successfully reproduced by photoreduction of DADH in the presence of 4-methyl-2-oxopentanoic acid (ketoleucine). The iminoleucine may be released readily due to weak interactions in the binding site, in contrast to iminoarginine, converted to ketoleucine, which reacts with activated FAD to form the covalently linked acyl adduct.
Authors:
Guoxing Fu; Hongling Yuan; Siming Wang; Giovanni Gadda; Irene T Weber
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-6-27
Journal Detail:
Title:  Biochemistry     Volume:  -     ISSN:  1520-4995     ISO Abbreviation:  -     Publication Date:  2011 Jun 
Date Detail:
Created Date:  2011-6-28     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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