Document Detail


Preliminary report of NAD+-dependent amino acid dehydrogenase producing bacteria isolated from soil.
MedLine Citation:
PMID:  18051956     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
BACKGROUND: Amino acid dehydrogenases (L-amino acid: oxidoreductase deaminating; EC 1.4.1.X) are members of the wider superfamily of oxidoreductases that catalyze the reversible oxidative deamination of an amino acid to its keto acid and ammonia with the concomitant reduction of either NAD+, NADP+ or FAD. These enzymes have been received much attention as biocatalysts for use in biosensors or diagnostic kits to screen amino acid metabolism disorders such as phenylketonuria (PKU), maple syrup urine disease (MSUD), homocystinuria (HCY) and hyperprolinemia. This study was aimed to isolation and screening of novel amino acid dehydrogenases from soil bacteria. METHODS: The enzyme producing bacteria were selected among L-methionine and L-phenylalanine utilizers isolated from soil by thin layer chromatography, activity staining and confirmed by enzyme assay. Bacterial strains were identified by phenotypic and biochemical characteristics. The steady-state kinetic studies of enzymes were also performed. RESULTS: In total of 230 tested strains, four of them were recognized as amino acid dehydrogenase producers that belong to species of Pseudomonas, Citrobacter and Proteus. They exhibited the desired NAD+-dependent dehydrogenase activities toward L-isoleucine, L-methionine, L-cysteine, L-serine and L-glutamine in oxidative deamination reaction. The specific activity of L-isoleucine dehydrogenase, L-methionine dehydrogenase and L-glutamine dehydrogenase for oxidative deamination of L-isoleucine, L-methionine and L-glutamine were 1.59, 1.2 and 0.73 U/mg, respectively. The Kcat/Km (s(-1).mM(-1)) values in these strains were as follows: L-isoleucine, 113.6, L-methionine, 62.05 and L-glutamine, 95.83. CONCLUSION: This is the first report of occurrence a specific isoleucine dehydrogenase, glutamine dehydrogenase and methionine dehydrogenase in bacteria.
Authors:
Hamid Shahbaz Mohammadi; Eskander Omidinia; Abbas Sahebghadam Lotfi; Reza Saghiri
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Iranian biomedical journal     Volume:  11     ISSN:  1028-852X     ISO Abbreviation:  Iran. Biomed. J.     Publication Date:  2007 Apr 
Date Detail:
Created Date:  2007-12-06     Completed Date:  2008-01-23     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9814853     Medline TA:  Iran Biomed J     Country:  Iran    
Other Details:
Languages:  eng     Pagination:  131-5     Citation Subset:  IM    
Affiliation:
Young Researcher Club, Dept. of Biochemistry, Science & Research Campus, Islamic Azad University, Tehran, Iran.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Oxidoreductases / isolation & purification,  metabolism*
Amino Acids / metabolism
Bacteria / enzymology*,  isolation & purification
Gram-Negative Bacteria / enzymology,  isolation & purification
Gram-Positive Bacteria / enzymology,  isolation & purification
Kinetics
NAD / metabolism*
Soil Microbiology*
Chemical
Reg. No./Substance:
0/Amino Acids; 53-84-9/NAD; EC 1.4.-/Amino Acid Oxidoreductases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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