Experimental characterization of two archaeal inosine 5'-monophosphate cyclohydrolases
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...
متن کاملProduction of guanosine-5'-monophosphate and inosine-5'-monophosphate by fermentation.
A biotin-requiring coryneform bacterium which produces glutamic acid was mutated to adenine dependency. The adenine-requiring strain, which excreted insoine-5'-monophosphate (IMP), was further mutated to xanthine dependency. As expected, IMP was also excreted by this mutant. The mutant strain was reverted to xanthine independence in an attempt to obtain a culture with an altered IMP dehydrogena...
متن کاملA Kinetic Alignment of Orthologous Inosine-5′-monophosphate Dehydrogenases†
IMP dehydrogenase (IMPDH) catalyzes two very different chemical transformations, a dehydrogenase reaction and a hydrolysis reaction. The enzyme toggles between the open conformation required for the dehydrogenase reaction and the closed conformation of the hydrolase reaction by moving a mobile flap into the NAD site. Despite these multiple functional constraints, the residues of the flap and NA...
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: PLOS ONE
سال: 2019
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0223983