Citramalate lyase

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citramalate lyase
Identifiers
EC no. 4.1.3.22
CAS no. 9027-93-4
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BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
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Gene Ontology AmiGO / QuickGO
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The enzyme citramalate lyase (EC 4.1.3.22) catalyzes the chemical reaction

(2S)-2-hydroxy-2-methylbutanedioate acetate + pyruvate

This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is (2S)-2-hydroxy-2-methylbutanedioate pyruvate-lyase (acetate-forming). Other names in common use include citramalate pyruvate-lyase, citramalate synthase, citramalic-condensing enzyme, citramalate synthetase, citramalic synthase, (S)-citramalate lyase, (+)-citramalate pyruvate-lyase, citramalate pyruvate lyase, (3S)-citramalate pyruvate-lyase, and (2S)-2-hydroxy-2-methylbutanedioate pyruvate-lyase. This enzyme participates in c5-branched dibasic acid metabolism.

Related Research Articles

<span class="mw-page-title-main">Glyoxylate cycle</span>

The glyoxylate cycle, a variation of the tricarboxylic acid cycle, is an anabolic pathway occurring in plants, bacteria, protists, and fungi. The glyoxylate cycle centers on the conversion of acetyl-CoA to succinate for the synthesis of carbohydrates. In microorganisms, the glyoxylate cycle allows cells to use two carbons, such as acetate, to satisfy cellular carbon requirements when simple sugars such as glucose or fructose are not available. The cycle is generally assumed to be absent in animals, with the exception of nematodes at the early stages of embryogenesis. In recent years, however, the detection of malate synthase (MS) and isocitrate lyase (ICL), key enzymes involved in the glyoxylate cycle, in some animal tissue has raised questions regarding the evolutionary relationship of enzymes in bacteria and animals and suggests that animals encode alternative enzymes of the cycle that differ in function from known MS and ICL in non-metazoan species.

<span class="mw-page-title-main">Mixed acid fermentation</span> Biochemical conversion of six-carbon sugars into acids in bacteria

In biochemistry, mixed acid fermentation is the metabolic process by which a six-carbon sugar is converted into a complex and variable mixture of acids. It is an anaerobic (non-oxygen-requiring) fermentation reaction that is common in bacteria. It is characteristic for members of the Enterobacteriaceae, a large family of Gram-negative bacteria that includes E. coli.

<span class="mw-page-title-main">Acetolactate synthase</span> Class of enzymes

The acetolactate synthase (ALS) enzyme is a protein found in plants and micro-organisms. ALS catalyzes the first step in the synthesis of the branched-chain amino acids.

<span class="mw-page-title-main">Cystathionine beta-lyase</span> Enzyme

Cystathionine beta-lyase, also commonly referred to as CBL or β-cystathionase, is an enzyme that primarily catalyzes the following α,β-elimination reaction

In enzymology, a citramalate CoA-transferase is an enzyme that catalyzes the chemical reaction

The enzyme 4-hydroxy-2-oxoglutarate aldolase catalyzes the chemical reaction

<span class="mw-page-title-main">4-hydroxy-2-oxovalerate aldolase</span> InterPro Family

The enzyme 4-hydroxy-2-oxovalerate aldolase catalyzes the chemical reaction

The enzyme 4-hydroxy-4-methyl-2-oxoglutarate aldolase catalyzes the chemical reaction

<span class="mw-page-title-main">Anthranilate synthase</span>

The enzyme anthranilate synthase catalyzes the chemical reaction

The enzyme citramalyl-CoA lyase catalyzes the chemical reaction

<span class="mw-page-title-main">Citrate (pro-3S)-lyase</span>

The enzyme citrate (pro-3S)-lyase catalyzes the chemical reaction

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

Isocitrate lyase, or ICL, is an enzyme in the glyoxylate cycle that catalyzes the cleavage of isocitrate to succinate and glyoxylate. Together with malate synthase, it bypasses the two decarboxylation steps of the tricarboxylic acid cycle and is used by bacteria, fungi, and plants.

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

The enzyme methylisocitrate lyase catalyzes the chemical reaction

<span class="mw-page-title-main">Oxalyl-CoA decarboxylase</span>

The enzyme oxalyl-CoA decarboxylase (OXC) (EC 4.1.1.8), primarily produced by the gastrointestinal bacterium Oxalobacter formigenes, catalyzes the chemical reaction

The enzyme (S)-2-methylmalate dehydratase (EC 4.2.1.34) catalyzes the chemical reaction:

In enzymology, a 2-isopropylmalate synthase (EC 2.3.3.13) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Malate synthase</span> Class of enzymes

In enzymology, a malate synthase (EC 2.3.3.9) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">DAHP synthase</span> Class of enzymes

3-Deoxy-D-arabinoheptulosonate 7-phosphate (DAHP) synthase is the first enzyme in a series of metabolic reactions known as the shikimate pathway, which is responsible for the biosynthesis of the amino acids phenylalanine, tyrosine, and tryptophan. Since it is the first enzyme in the shikimate pathway, it controls the amount of carbon entering the pathway. Enzyme inhibition is the primary method of regulating the amount of carbon entering the pathway. Forms of this enzyme differ between organisms, but can be considered DAHP synthase based upon the reaction that is catalyzed by this enzyme.

(R)-citramalate synthase (EC 2.3.1.182, CimA) is an enzyme. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Dihydrodipicolinate synthase</span> Class of enzymes

4-Hydroxy-tetrahydrodipicolinate synthase (EC 4.3.3.7, dihydrodipicolinate synthase, dihydropicolinate synthetase, dihydrodipicolinic acid synthase, L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and cyclizing), dapA (gene)) is an enzyme with the systematic name L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and cyclizing; (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate-forming). This enzyme catalyses the following chemical reaction

References