C
Cuneyt M. Serdar
Researcher at University of Texas at Austin
Publications - 5
Citations - 452
Cuneyt M. Serdar is an academic researcher from University of Texas at Austin. The author has contributed to research in topics: Plasmid & Pseudomonas putida. The author has an hindex of 5, co-authored 5 publications receiving 444 citations.
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Journal ArticleDOI
Plasmid Involvement in Parathion Hydrolysis by Pseudomonas diminuta
TL;DR: An organism identified as Pseudomonas diminuta was found to hydrolyze parathion and hydrolase-negative derivatives were missing a plasmid present in the wild-type organism.
Journal ArticleDOI
Enzymatic Hydrolysis of Organophosphates: Cloning and Expression of a Parathion Hydrolase Gene from Pseudomonas diminuta
Cuneyt M. Serdar,David T. Gibson +1 more
TL;DR: Pseudomonas diminuta strain MG hydrolyzes parathion to diethylthiophosphoric acid and p-nitrophenol and the esterase responsible for this reaction is encoded by a gene located on a plasmid termed pCMS1, which resulted in the isolation of transconjugants that exhibitedParathion hydrolase activity.
Journal ArticleDOI
Studies of nucleotide sequence homology between naphthalene-utilizing strains of bacteria
Cuneyt M. Serdar,David T. Gibson +1 more
TL;DR: The ability of P. putida, strain NCIB 9816, to grow with naphthalene (Nah+) and salicylate (Sal+) is correlated with the presence of an 83 kilobase (kb) conjugative plasmid (pDTG1) which is cloned into pKT230, which was nick-translated and used as a radioactive probe to investigate nucleotide sequence homology.
Journal ArticleDOI
Isolation and characterization of altered plasmids in mutant strains of Pseudomonas putida NCIB 9816.
Cuneyt M. Serdar,David T. Gibson +1 more
TL;DR: The ability of P. putida NCIB 9816 to grow with naphthalene (Nah+) and salicylate (Sal+) is correlated with the presence of an 83 kilobase (kb) conjugative plasmid, pDTG1, and the structural changes in mutant plasmids were correlated withthe absence of essential enzymatic activities.
Purification and Properties of FerredoxinToL
Venkiteswaran SubramanianS,Te-Ning Liuji,Wu-Kuang Yehll,Cuneyt M. Serdar,Lawrence P. Wackett,David T. Gibson +5 more
TL;DR: Anaerobic reductive titrations revealed that ferredoxinToL is a one-electron carrier that accepts electrons from NADH in a reaction that is mediated by a flavoprotein (ferredoxin toL reductase), the first component in the toluene dioxygenase system.