2003ACS symposium seriesRequires access

Inosine Monophosphate Dehydrogenase

Krzysztof W. Pankiewicz, Barry Goldstein

Open publisher page 29 citations

Abstract

Inosine 5'-monophosphate dehydrogenase (IMPDH, E.C.1.1.1.205), the NADdependent enzyme that controls de novo synthesis of purine nucleotides, catalyzes the oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5'-monophosphate (XMP), which is then converted to guanosine 5'-monophosphate (GMP) by GMP synthase (Fig.1). IMP also serves as a substrate for the biosynthesis of adenosine 5'-monophosphate (AMP). An adequate pool of purine nucleotides is essential for cell proliferation, cell signaling, and as an energy source. Consequently, inhibition of IMPDH causes a variety of biological responses, and it is not surprising that this enzyme has emerged as a major target for antiviral, antileukemic and immunosuppressive therapies.

About this research paper

What this paper is about

Inosine 5'-monophosphate dehydrogenase (IMPDH, E.C.1.1.1.205), the NADdependent enzyme that controls de novo synthesis of purine nucleotides, catalyzes the oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5'-monophosphate (XMP), which is then converted to guanosine 5'-monophosphate (GMP) by GMP synthase (Fig.1). IMP also serves as a substrate for the biosynthesis of adenosine 5'-monophosphate (AMP). An adequate pool of purine nucleotides is essential for cell proliferation, cell signaling, and as an energy source. Consequently, inhibition of IMPDH causes a variety of biological responses, and it is not surprising that this enzyme has emerged as a major target for antiviral, antileukemic and immunosuppressive therapies.

Why it matters

OpenAlex reports 29 citations for this work. Citation counts describe recorded attention and do not establish research quality.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

Inosine 5'-monophosphate dehydrogenase (IMPDH, E.C.1.1.1.205), the NADdependent enzyme that controls de novo synthesis of purine nucleotides, catalyzes the oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5'-monophosphate (XMP), which is then converted to guanosine 5'-monophosphate (GMP) by GMP synthase (Fig.1). IMP also serves as a substrate for the biosynthesis of adenosine 5'-monophosphate (AMP). An adequate pool of purine nucleotides is essential for cell proliferation, cell signaling, and as an energy source. Consequently, inhibition of IMPDH causes a variety of biological responses, and it is not surprising that this enzyme has emerged as a major target for antiviral, antileukemic and immunosuppressive therapies.

Key concepts: IMP dehydrogenase, Guanosine monophosphate, Inosine monophosphate, Inosine, Purine metabolism, Biochemistry, Nucleotide, Guanosine

Related papers

Back to paper searchBrowse research topicsOriginal source
Inosine Monophosphate Dehydrogenase — Research Paper | ScholarLens