D-glutamate cyclase

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D-glutamate cyclase
Identifiers
EC no. 4.2.1.48
CAS no. 37290-80-5
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MetaCyc metabolic pathway
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The enzyme D-glutamate cyclase (EC 4.2.1.48) catalyzes the chemical reaction

D-glutamate 5-oxo-Dproline + H2O

This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is D-glutamate hydro-lyase (cyclizing; 5-oxo-D-proline-forming). This enzyme is also called D-glutamate hydro-lyase (cyclizing). This enzyme participates in D-glutamine and D-glutamate metabolism.

Related Research Articles

In biochemistry, a lyase is an enzyme that catalyzes the breaking of various chemical bonds by means other than hydrolysis and oxidation, often forming a new double bond or a new ring structure. The reverse reaction is also possible. For example, an enzyme that catalyzed this reaction would be a lyase:

<span class="mw-page-title-main">Fumarase</span> Type of enzyme

Fumarase is an enzyme that catalyzes the reversible hydration/dehydration of fumarate to malate. Fumarase comes in two forms: mitochondrial and cytosolic. The mitochondrial isoenzyme is involved in the Krebs cycle and the cytosolic isoenzyme is involved in the metabolism of amino acids and fumarate. Subcellular localization is established by the presence of a signal sequence on the amino terminus in the mitochondrial form, while subcellular localization in the cytosolic form is established by the absence of the signal sequence found in the mitochondrial variety.

In enzymology, a glutamate-5-semialdehyde dehydrogenase (EC 1.2.1.41) is an enzyme that catalyzes the chemical reaction

In enzymology, a N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38) is an enzyme that catalyzes the chemical reaction

In enzymology, a formimidoyltetrahydrofolate cyclodeaminase (EC 4.3.1.4) is an enzyme that catalyzes the chemical reaction

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

The enzyme anthranilate synthase 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

The enzyme citryl-CoA 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.

The enzyme oxalomalate lyase catalyzes the chemical reaction

The enzyme 5-dehydro-4-deoxyglucarate dehydratase (EC 4.2.1.41) catalyzes the chemical reaction

The enzyme altronate dehydratase (EC 4.2.1.7) catalyzes the chemical reaction

<span class="mw-page-title-main">Glucarate dehydratase</span>

The enzyme glucarate dehydratase (EC 4.2.1.40) catalyzes the chemical reaction

The enzyme hydroperoxide dehydratase (EC 4.2.1.92) catalyzes the chemical reaction

The enzyme oleate hydratase (EC 4.2.1.53) catalyzes the chemical reaction

The enzyme protoaphin-aglucone dehydratase (cyclizing) (EC 4.2.1.73) catalyzes the chemical reaction

In enzymology, a 5-oxoprolinase (ATP-hydrolysing) (EC 3.5.2.9) is an enzyme that catalyzes the 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

Arginine and proline metabolism is one of the central pathways for the biosynthesis of the amino acids arginine and proline from glutamate. The pathways linking arginine, glutamate, and proline are bidirectional. Thus, the net utilization or production of these amino acids is highly dependent on cell type and developmental stage. Altered proline metabolism has been linked to metastasis formation in breast cancer.

References


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