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Molecular and Kinetic Characterization of the Aspartate Transcarbamoylase Dihydroorotase Complex in Pseudomonas putida

Aerobic Gram negative bacteria such as Pseudomonas putida were reported to possess class A ATCases and to have a M.W. of 360 kD. The nucleotide sequence of the P. putida pyrBC was determined to answer this question once and for all. The expected regulatory gene was not found. It is shown that the P. putida pyrB gene is overlapped by pyrC by 4 bp. The P.putida pyrB is 1005 bp (335 aa) in length and the pyrC is 1275 bp (425 aa) long. Both of these genes complement E. coli mutants with their respective genotypes. Another finding borne out from the sequence is an effector binding site at the N-terminus of pyrB of P. putIda. The binding site shows that effectors compete with carbamoylphosphate for the active site. In this dissertation, it is shown that the ATCase of P.putida is a trimer of M.W. of 109 kD (3 x 36.4 kD) and that the gene encoding pyrB is overlapped by the pyrC gene which encodes DHOase. It is also shown that the pyrBC encoded enzymes copurify as a dodecameric complex with a M.W. of 484 kD.

Identiferoai:union.ndltd.org:unt.edu/info:ark/67531/metadc277575
Date05 1900
CreatorsSchurr, Michael J. (Michael John)
ContributorsO'Donovan, Gerard A., Shanley, Mark Stephen, Benjamin, Robert C., Kunz, Daniel A., Knesek, John
PublisherUniversity of North Texas
Source SetsUniversity of North Texas
LanguageEnglish
Detected LanguageEnglish
TypeThesis or Dissertation
Formatviii, 181 leaves : ill., Text
RightsPublic, Copyright, Copyright is held by the author, unless otherwise noted. All rights reserved., Schurr, Michael J. (Michael John)

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