Aspartate ammonia-lyase

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aspartate ammonia-lyase
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Aspartate ammonia-lyase homotetramer, Bacillus sp. YM55-1
Identifiers
EC no. 4.3.1.1
CAS no. 9027-30-9
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ExPASy NiceZyme view
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MetaCyc metabolic pathway
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The enzyme aspartate ammonia-lyase (EC 4.3.1.1) catalyzes the chemical reaction

L-aspartate fumarate + NH3

The reaction is the basis of the industrial synthesis of aspartate. [1]

This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is L-aspartate ammonia-lyase (fumarate-forming). Other names in common use include aspartase, fumaric aminase, L-aspartase, and L-aspartate ammonia-lyase. This enzyme participates in alanine and aspartate metabolism and nitrogen metabolism.

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1J3U and 1JSW.

Related Research Articles

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<span class="mw-page-title-main">Argininosuccinate lyase</span> Mammalian protein found in Homo sapiens

The enzyme argininosuccinate lyase (EC 4.3.2.1, ASL, argininosuccinase; systematic name 2-(N ω-L-arginino)succinate arginine-lyase (fumarate-forming)) catalyzes the reversible breakdown of argininosuccinate:

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The enzyme β-Alanyl-CoA ammonia-lyase (EC 4.3.1.6) catalyzes the chemical reaction

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

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<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">Methylaspartate ammonia-lyase</span>

The enzyme methylaspartate ammonia-lyase (EC 4.3.1.2) catalyzes the chemical reaction

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

The enzyme phenylalanine ammonia lyase (EC 4.3.1.24) catalyzes the conversion of L-phenylalanine to ammonia and trans-cinnamic acid.:

The enzyme threo-3-hydroxyaspartate ammonia-lyase (EC 4.3.1.16) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Aspartate 1-decarboxylase</span>

The enzyme aspartate 1-decarboxylase (EC 4.1.1.11) catalyzes the chemical reaction

<span class="mw-page-title-main">Aspartate 4-decarboxylase</span>

In enzymology, an aspartate 4-decarboxylase (EC 4.1.1.12) is an enzyme that catalyzes the chemical reaction

The enzyme orsellinate decarboxylase (EC 4.1.1.58) catalyzes the chemical reaction

<span class="mw-page-title-main">Tryptophanase</span> Enzyme that converts tryptophan into indole

The enzyme tryptophanase (EC 4.1.99.1) catalyzes the chemical reaction

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Fumarate lyase belongs to the lyase class of enzymes. These proteins use fumarate as a substrate. They have been shown to share a short conserved sequence around a methionine which is probably involved in the catalytic activity of this type of enzymes.

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

The Purine Nucleotide Cycle is a metabolic pathway in protein metabolism requiring the amino acids aspartate and glutamate. The cycle is used to regulate the levels of adenine nucleotides, in which ammonia and fumarate are generated. AMP coverts into IMP and the byproduct ammonia. IMP converts to S-AMP (adenylosuccinate), which then coverts to AMP and the byproduct fumarate. The fumarate goes on to produce ATP (energy) via oxidative phosphorylation as it enters the Krebs cycle and then the electron transport chain. Lowenstein first described this pathway and outlined its importance in processes including amino acid catabolism and regulation of flux through glycolysis and the Krebs cycle.

References

  1. Karlheinz Drauz; Ian Grayson; Axel Kleemann; Hans-Peter Krimmer; Wolfgang Leuchtenberger; Christoph Weckbecker (2006). "Amino Acids". Ullmann's Encyclopedia of Industrial Chemistry . Weinheim: Wiley-VCH. doi:10.1002/14356007.a02_057.pub2.