Isocitrate epimerase

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Isocitrate epimerase
Identifiers
EC no. 5.1.2.6
CAS no. 81210-68-6
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MetaCyc metabolic pathway
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In enzymology, an isocitrate epimerase is classified as follows: EC 5.1.2.6. This number indicates that it is an isomerase, specifically a racemase or epimerase that acts on hydroxy acids and their derivatives, namely isocitrate. [1] Isocitrate epimerase specifically catalyzes the reversible reaction: [2]

(1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate ↔ (1S,2S)-1-hydroxypropane-1,2,3-tricarboxylate

which can also be described as

D-threo-isocitrate ↔ D-erythro-isocitrate
D-threo-isocitrate = D-erythro-isocitrate.png

History

Isocitrate epimerase was originally isolated from the fungal cell-free extract of Penicillium purpurogenum [3] , where it was discovered due to the excess accumulation of L-alloisocitric acid (D-erythro-isocitrate)—a diastereomer of isocitrate previously not seen in nature. In order to accumulate L-alloisocitric acid as a fermentation product, P. purpurogenum needed to be grown on citrate supplemented nutrient agar. [3] [4] During this fermentation it was found that the fermentation yield of L-alloisocitric acid was capable of “exceeding 70% without producing any other stereoisomers of isocitiric acid or other metabolites”. [3]

This enzyme has not been heavily studied since first being identified in 1982, as a result of this there is presently not a crystal structure or active site description for isocitrate epimerase. Other isocitrate enzymes, such as isocitrate lyase and isocitrate dehydrogenase have been studied more closely due to their key roles in glycolysis and the TCA cycle.

Related Research Articles

<span class="mw-page-title-main">Citric acid cycle</span> Chemical reactions to release energy in cells

The citric acid cycle —also known as the Krebs cycle, Szent-Györgyi-Krebs cycle or the TCA cycle (tricarboxylic acid cycle)—is a series of chemical reactions to release stored energy through the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins. The Krebs cycle is used by organisms that respire (as opposed to organisms that ferment) to generate energy, either by anaerobic respiration or aerobic respiration. In addition, the cycle provides precursors of certain amino acids, as well as the reducing agent NADH, that are used in numerous other reactions. Its central importance to many biochemical pathways suggests that it was one of the earliest components of metabolism. Even though it is branded as a 'cycle', it is not necessary for metabolites to follow only one specific route; at least three alternative segments of the citric acid cycle have been recognized.

<span class="mw-page-title-main">Isocitrate dehydrogenase</span> Class of enzymes

Isocitrate dehydrogenase (IDH) (EC 1.1.1.42) and (EC 1.1.1.41) is an enzyme that catalyzes the oxidative decarboxylation of isocitrate, producing alpha-ketoglutarate (α-ketoglutarate) and CO2. This is a two-step process, which involves oxidation of isocitrate (a secondary alcohol) to oxalosuccinate (a ketone), followed by the decarboxylation of the carboxyl group beta to the ketone, forming alpha-ketoglutarate. In humans, IDH exists in three isoforms: IDH3 catalyzes the third step of the citric acid cycle while converting NAD+ to NADH in the mitochondria. The isoforms IDH1 and IDH2 catalyze the same reaction outside the context of the citric acid cycle and use NADP+ as a cofactor instead of NAD+. They localize to the cytosol as well as the mitochondrion and peroxisome.

BRENDA is an information system representing one of the most comprehensive enzyme repositories. It is an electronic resource that comprises molecular and biochemical information on enzymes that have been classified by the IUBMB. Every classified enzyme is characterized with respect to its catalyzed biochemical reaction. Kinetic properties of the corresponding reactants are described in detail. BRENDA contains enzyme-specific data manually extracted from primary scientific literature and additional data derived from automatic information retrieval methods such as text mining. It provides a web-based user interface that allows a convenient and sophisticated access to the data.

<span class="mw-page-title-main">Phosphopentose epimerase</span>

Phosphopentose epimerase encoded by the RPE gene is a metalloprotein that catalyzes the interconversion between D-ribulose 5-phosphate and D-xylulose 5-phosphate.

Translocase is a general term for a protein that assists in moving another molecule, usually across a cell membrane. These enzymes catalyze the movement of ions or molecules across membranes or their separation within membranes. The reaction is designated as a transfer from “side 1” to “side 2” because the designations “in” and “out”, which had previously been used, can be ambiguous. Translocases are the most common secretion system in Gram positive bacteria.

<span class="mw-page-title-main">Homoisocitrate dehydrogenase</span> Enzyme

In enzymology, a homoisocitrate dehydrogenase (EC 1.1.1.87) is an enzyme that catalyzes the chemical reaction

In enzymology, an amino-acid racemase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Diaminopimelate epimerase</span>

In enzymology, a diaminopimelate epimerase is an enzyme that catalyzes the chemical reaction

In enzymology, an isopenicillin N epimerase is an enzyme that catalyzes the chemical reaction

In enzymology, a protein-serine epimerase is an enzyme that catalyzes the chemical reaction

In enzymology, an UDP-glucuronate 4-epimerase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Dihydroneopterin aldolase</span>

The enzyme dihydroneopterin aldolase catalyzes the chemical reaction

<span class="mw-page-title-main">Methylisocitrate lyase</span>

The enzyme methylisocitrate lyase catalyzes the chemical reaction

The enzyme 2-methylcitrate dehydratase (EC 4.2.1.79) catalyzes the chemical reaction

The enzyme 2-methylisocitrate dehydratase (EC 4.2.1.99) catalyzes the chemical reaction

<span class="mw-page-title-main">Homoaconitate hydratase</span> Enzyme

The enzyme homoaconitate hydratase (EC 4.2.1.36) catalyzes the chemical reaction

In enzymology, a 2-methylcitrate synthase (EC 2.3.3.5) is an enzyme that catalyzes the chemical reaction

Decylcitrate synthase (EC 2.3.3.2) is an enzyme that catalyzes the chemical reaction in enzymology.

In enzymology, a decylhomocitrate synthase (EC 2.3.3.4) is an enzyme that catalyzes the chemical reaction

In enzymology, an isocitrate O-dihydroxycinnamoyltransferase is an enzyme that catalyzes the chemical reaction

References

  1. "BRENDA - Information on EC 5.1.2.6 - isocitrate epimerase". www.brenda-enzymes.org. Retrieved 2021-10-22.
  2. "KEGG REACTION: R02318". www.genome.jp. Retrieved 2021-10-22.
  3. 1 2 3 Hoshiko S, Kunimoto Y, Arima K, Beppu T (January 1982). "Mechanism of L-Alloisocitric Acid Fermentation: Isocitrate Epimerase Activity in the Cell-free Extract of Penicillium purpurogenum". Agricultural and Biological Chemistry. 46 (1): 143–151. doi:10.1080/00021369.1982.10865025. ISSN   0002-1369.
  4. Beppu T, Abe S, Sakaguchi K (December 2004). "Accumulation of allo-isocitric acid by a Penicillium strain". The Journal of General and Applied Microbiology. 50 (6): 345–352. PMID   15965889.