ArticleProceedings of the National Academy of Sciences of the United States of America2001
Structural genomics of enzymes involved in sterol/isoprenoid biosynthesis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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38 citing papers in PubMed, 114 citations in OpenAlex.
- The Mevalonate Pathway: Innovations, Applications, and Challenges in Biotechnology with Emphasis on Fungal Biology.Journal of fungi (Basel, Switzerland) · 2026Review
- Engineering ofMetabolic engineering communications · 2022Review
- A cryptic activity in the Nudix hydrolase superfamily.Protein science : a publication of the Protein Society · 2019Article
- A Single Amino Acid Mutation Converts (The Journal of biological chemistry · 2017Article
- A novel plant enzyme with dual activity: an atypical Nudix hydrolase and a dipeptidyl peptidase III.Biological chemistry · 2017Article
- An Adaptation To Life In Acid Through A Novel Mevalonate Pathway.Scientific reports · 2016Article
- The Genomes of Three Uneven Siblings: Footprints of the Lifestyles of Three Trichoderma Species.Microbiology and molecular biology reviews : MMBR · 2016Review
- Active site binding modes of inhibitors of Staphylococcus aureus mevalonate diphosphate decarboxylase from docking and molecular dynamics simulations.Journal of molecular modeling · 2016Article
- In Vivo Formation of the Protein Disulfide Bond That Enhances the Thermostability of Diphosphomevalonate Decarboxylase, an Intracellular Enzyme from the Hyperthermophilic Archaeon Sulfolobus solfataricus.Journal of bacteriology · 2015Article
- Isolation, characterization and antifungal docking studies of wortmannin isolated from Penicillium radicum.Scientific reports · 2015Article
- Structural analysis of mevalonate-3-kinase provides insight into the mechanisms of isoprenoid pathway decarboxylases.Protein science : a publication of the Protein Society · 2015Article
- Mechanistic differences between nucleic acid chaperone activities of the Gag proteins of Rous sarcoma virus and human immunodeficiency virus type 1 are attributed to the MA domain.Journal of virology · 2014Article
- Metabolic engineering of Escherichia coli for high-specificity production of isoprenol and prenol as next generation of biofuels.Biotechnology for biofuels · 2013Article
- Structural basis of functional group activation by sulfotransferases in complex metabolic pathways.ACS chemical biology · 2012Article
- Characterization of an isopentenyl diphosphate isomerase involved in the juvenile hormone pathway in Aedes aegypti.Insect biochemistry and molecular biology · 2012Article
- Structural basis for nucleotide binding and reaction catalysis in mevalonate diphosphate decarboxylase.Biochemistry · 2012Article
- The Protein Structure Initiative: achievements and visions for the future.F1000 biology reports · 2012Article
- Crystal structures of Staphylococcus epidermidis mevalonate diphosphate decarboxylase bound to inhibitory analogs reveal new insight into substrate binding and catalysis.The Journal of biological chemistry · 2011Article
- Enzymes of the mevalonate pathway of isoprenoid biosynthesis.Archives of biochemistry and biophysics · 2011Review
- Terpene Specialized Metabolism in Arabidopsis thaliana.The arabidopsis book · 2011Article
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11 authors at 3 institutions in 1 country.
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Abstract
X-ray structures of two enzymes in the sterol/isoprenoid biosynthesis pathway have been determined in a structural genomics pilot study. Mevalonate-5-diphosphate decarboxylase (MDD) is a single-domain alpha/beta protein that catalyzes the last of three sequential ATP-dependent reactions which convert mevalonate to isopentenyl diphosphate. Isopentenyl disphosphate isomerase (IDI) is an alpha/beta metalloenzyme that catalyzes interconversion of isopentenyl diphosphate and dimethylallyl diphosphate, which condense in the next step toward synthesis of sterols and a host of natural products. Homology modeling of related proteins and comparisons of the MDD and IDI structures with two other experimentally determined structures have shown that MDD is a member of the GHMP superfamily of small-molecule kinases and IDI is similar to the nudix hydrolases, which act on nucleotide diphosphatecontaining substrates. Structural models were produced for 379 proteins, encompassing a substantial fraction of both protein superfamilies. All three enzymes responsible for synthesis of isopentenyl diphosphate from mevalonate (mevalonate kinase, phosphomevalonate kinase, and MDD) share the same fold, catalyze phosphorylation of chemically similar substrates (MDD decarboxylation involves phosphorylation of mevalonate diphosphate), and seem to have evolved from a common ancestor. These structures and the structural models derived from them provide a framework for interpreting biochemical function and evolutionary relationships.
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