Carbamoyl phosphate synthetase (CPS) catalyzes the formation of carbamoyl
phosphate (CP) from MgATP, bicarbonate, and glutamine. It has three active sites, one
present on the small subunit and the two phosphorylation sites present on the large
subunit. These two nucleotide binding sites are homologous. Six compounds were
designed to mimic the reactive intermediate species carboxy phosphate, and product
cabamoyl phosphate. The apparent Ki values calculated estimated the inhibitory strengths
of these compounds. These plots were also utilized in identifying the linear inhibitors,
nonlinear inhibitors and partial inhibitors. Inhibition patterns were obtained with these
compounds using various assay formats. Partial inhibition displayed by phosphono
formate for the full biosynthetic reaction can be utilized in support of the sequential
mechanism for CPS.
| Identifer | oai:union.ndltd.org:tamu.edu/oai:repository.tamu.edu:1969.1/4810 |
| Date | 25 April 2007 |
| Creators | Tripathi, Neha |
| Contributors | Raushel, Frank M. |
| Publisher | Texas A&M University |
| Source Sets | Texas A and M University |
| Language | en_US |
| Detected Language | English |
| Type | Book, Thesis, Electronic Thesis, text |
| Format | 400283 bytes, electronic, application/pdf, born digital |
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