The CBS subdomain of inosine 5′-monophosphate dehydrogenase regulates purine nucleotide turnover
نویسندگان
چکیده
منابع مشابه
Inosine 5 0 - Monophosphate Dehydrogenase
I. Overview of IMPDH A. Protein Structures II. Medicinal Applications of IMPDH Inhibitors A. IMP Analogs B. NAD Analogs C. Natural Product Inhibitors D. Novel Synthetic Inhibitors III. Kinetic Mechanism and Substrate Interactions A. Case Studies 1. Tritrichomonas foetus IMPDH 2. Escherichia coli IMPDH 3. Human IMPDH B. Ligand Binding 1. IMP Binding Site 2. NAD Binding Site IV. Chemical Mechanis...
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Today’s medical word is highly dependent on severel natural products (e.g. taxol) in fighting different kinds of cancer and in constantly working to found new compounds. In this respect, 3-hydrogenkwadaphnin is a new diterpene ester isolated from Dendrostellera lessertii (Thymelaceae). It has been previously shown that this new compound has high anti-tumor activity and the capability of arresti...
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Today’s medical word is highly dependent on severel natural products (e.g. taxol) in fighting different kinds of cancer and in constantly working to found new compounds. In this respect, 3-hydrogenkwadaphnin is a new diterpene ester isolated from Dendrostellera lessertii (Thymelaceae). It has been previously shown that this new compound has high anti-tumor activity and the capability of arresti...
متن کاملCharacteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase.
IMP dehydrogenase (IMPDH) is an essential enzyme that catalyzes the first step unique to GTP synthesis. To provide a basis for the evaluation of IMPDH inhibitors as antimicrobial agents, we have expressed and characterized IMPDH from the pathogenic bacterium Streptococcus pyogenes. Our results show that the biochemical and kinetic characteristics of S. pyogenes IMPDH are similar to other bacter...
متن کاملStructure of Pseudomonas aeruginosa inosine 5′-monophosphate dehydrogenase
Inosine 5'-monophosphate dehydrogenase (IMPDH) represents a potential antimicrobial drug target. The crystal structure of recombinant Pseudomonas aeruginosa IMPDH has been determined to a resolution of 2.25 Å. The structure is a homotetramer of subunits dominated by a (β/α)8-barrel fold, consistent with other known structures of IMPDH. Also in common with previous work, the cystathionine β-synt...
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ژورنال
عنوان ژورنال: Molecular Microbiology
سال: 2008
ISSN: 0950-382X
DOI: 10.1111/j.1365-2958.2008.06153.x