Glucosaminate ammonia-lyase

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glucosaminate ammonia-lyase
Identifiers
EC no. 4.3.1.9
CAS no. 37290-91-8
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MetaCyc metabolic pathway
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Gene Ontology AmiGO / QuickGO
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The enzyme Glucosaminate ammonia-lyase (EC 4.3.1.9) catalyzes the chemical reaction

2-amino-2-deoxy-D-gluconate = 2-dehydro-3-deoxy-D-gluconate + NH3 (overall reaction)
(1a) 2-amino-2-deoxy-Dgluconate = (2Z,4S,5R)-2-amino-4,5,6-trihydroxyhex-2-enoate + H2O
(1b) (2Z,4S,5R)-2-amino-4,5,6-trihydroxyhex-2-enoate = (4S,5R)-4,5,6-trihydroxy-2-iminohexanoate (spontaneous)
(1c) (4S,5R)-4,5,6-trihydroxy-2-iminohexanoate + H2O = 2-dehydro-3-deoxyD-gluconate + NH3 (spontaneous)

This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is 2-amino-2-deoxy-D-gluconate ammonia-lyase (isomerizing; 2-dehydro-3-deoxy-D-gluconate-forming). Other names in common use include glucosaminic dehydrase, D-glucosaminate dehydratase, D-glucosaminic acid dehydrase, aminodeoxygluconate dehydratase, 2-amino-2-deoxy-D-gluconate hydro-lyase (deaminating), aminodeoxygluconate ammonia-lyase, 2-amino-2-deoxy-D-gluconate ammonia-lyase, and D-glucosaminate ammonia-lyase. This enzyme participates in the pentose phosphate pathway. It employs one cofactor, pyridoxal phosphate.

Related Research Articles

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

Serine dehydratase or L-serine ammonia lyase (SDH) is in the β-family of pyridoxal phosphate-dependent (PLP) enzymes. SDH is found widely in nature, but its structural and properties vary among species. SDH is found in yeast, bacteria, and the cytoplasm of mammalian hepatocytes. SDH catalyzes is the deamination of L-serine to yield pyruvate, with the release of ammonia.

<span class="mw-page-title-main">Cystathionine gamma-lyase</span> Protein-coding gene in the species Homo sapiens

The enzyme cystathionine γ-lyase (EC 4.4.1.1, CTH or CSE; also cystathionase; systematic name L-cystathionine cysteine-lyase (deaminating; 2-oxobutanoate-forming)) breaks down cystathionine into cysteine, 2-oxobutanoate (α-ketobutyrate), and ammonia:

The enzyme carbamoyl-serine ammonia-lyase (EC 4.3.1.13) catalyzes the chemical reaction

The enzyme D-serine ammonia-lyase (EC 4.3.1.18), with systematic name D-serine ammonia-lyase (pyruvate-forming), catalyzes the chemical reaction

<span class="mw-page-title-main">L-serine ammonia-lyase</span>

The enzyme L-serine ammonia-lyase (EC 4.3.1.17) catalyzes the chemical reaction

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

Threonine ammonia-lyase (EC 4.3.1.19, systematic name L-threonine ammonia-lyase (2-oxobutanoate-forming), also commonly referred to as threonine deaminase or threonine dehydratase, is an enzyme responsible for catalyzing the conversion of L-threonine into α-ketobutyrate and ammonia:

The enzyme 5-dehydro-2-deoxyphosphogluconate aldolase 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

The enzyme galactarate dehydratase (EC 4.2.1.42) catalyzes the chemical reaction

The enzyme galactonate dehydratase (EC 4.2.1.6) catalyzes the chemical reaction

<span class="mw-page-title-main">GDP-mannose 4,6-dehydratase</span>

The enzyme GDP-mannose 4,6-dehydratase (EC 4.2.1.47) 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 gluconate dehydratase (EC 4.2.1.39) catalyzes the chemical reaction

The enzyme L-arabinonate dehydratase (EC 4.2.1.25) catalyzes the chemical reaction

The enzyme mannonate dehydratase (EC 4.2.1.8) catalyzes the chemical reaction

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

The enzyme phosphogluconate dehydratase (EC 4.2.1.12) catalyzes the chemical reaction

The enzyme xylonate dehydratase (EC 4.2.1.82) 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.

References