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Tryptophanase

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tryptophanase
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Tryptophanase tetramer, E.Coli
Identifiers
EC no. 4.1.99.1
CAS no. 9024-00-4
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The enzyme tryptophanase (EC 4.1.99.1) catalyzes the chemical reaction

Contents

L-tryptophan + H2O indole + pyruvate + NH3
Indole.svg

This enzyme belongs to the family of lyases, specifically in the "catch-all" class of carbon-carbon lyases. The systematic name of this enzyme class is L-tryptophan indole-lyase (deaminating; pyruvate-forming). Other names in common use include L-tryptophanase, and L-tryptophan indole-lyase (deaminating). This enzyme participates in tryptophan metabolism and nitrogen metabolism. It has 2 cofactors: pyridoxal phosphate, and potassium. [1] [2] [3]

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1AX4, [4] 2C44, [5] and 2OQX. [6]

Related Research Articles

<span class="mw-page-title-main">Tryptophan</span> Chemical compound

Tryptophan is an α-amino acid that is used in the biosynthesis of proteins. Tryptophan contains an α-amino group, an α-carboxylic acid group, and a side chain indole, making it a polar molecule with a non-polar aromatic beta carbon substituent. Tryptophan is also a precursor to the neurotransmitter serotonin, the hormone melatonin, and vitamin B3. It is encoded by the codon UGG.

Alanine dehydrogenase (EC 1.4.1.1) is an enzyme that catalyzes the chemical reaction

<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

The enzyme cysteine-S-conjugate β-lyase (EC 4.4.1.13) catalyzes the chemical reaction

The enzyme D-cysteine desulfhydrase (EC 4.4.1.15) 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">Methylaspartate ammonia-lyase</span>

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

<span class="mw-page-title-main">Ornithine cyclodeaminase</span>

The enzyme ornithine cyclodeaminase 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 4-hydroxy-2-oxoglutarate aldolase 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">Indole-3-glycerol-phosphate synthase</span> Class of enzymes

The enzyme indole-3-glycerol-phosphate synthase (IGPS) (EC 4.1.1.48) catalyzes the chemical reaction

The enzyme indolepyruvate decarboxylase (EC 4.1.1.74) catalyzes the chemical reaction

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

The enzyme N-acetylneuraminate lyase catalyzes the chemical reaction

The enzyme phenylpyruvate decarboxylase (EC 4.1.1.43) catalyzes the chemical reaction

The enzyme rhamnulose-1-phosphate aldolase (EC 4.1.2.19) catalyzes the chemical reaction

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

The enzyme threonine aldolase is an enzyme that catalyzes the chemical reaction

The enzyme tyrosine phenol-lyase (EC 4.1.99.2) 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">Tryptophan transaminase</span>

In enzymology, a tryptophan transaminase is an enzyme that catalyzes the chemical reaction

References

  1. ↑ BURNS RO, DEMOSS RD (1962). "Properties of tryptophanase from Escherichia coli". Biochim. Biophys. Acta. 65 (2): 233–44. doi:10.1016/0006-3002(62)91042-9. PMID   14017164.
  2. ↑ Cowell JL, Maser K, DeMoss, RD (1973). "Tryptophanase from Aeromonas liquifaciens. Purification, molecular weight and some chemical, catalytic and immunological properties". Biochimica et Biophysica Acta . 315: 449–463. doi:10.1016/0005-2744(73)90276-3.
  3. ↑ NEWTON WA, MORINO Y, SNELL EE (1965). "Properties of Crystalline Tryptophanase". J. Biol. Chem. 240 (3): 1211–8. doi: 10.1016/S0021-9258(18)97562-9 . PMID   14284727.
  4. ↑ 1AX4 Retrieved from Protein Data Bank (PDB)
  5. ↑ 2C44 Retrieved from Protein Data Bank (PDB)
  6. ↑ 2OQX Retrieved from Protein Data Bank (PDB)


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