Dihydroxyphenylalanine ammonia-lyase

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dihydroxyphenylalanine ammonia-lyase
Identifiers
EC no. 4.3.1.11
CAS no. 37290-92-9
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MetaCyc metabolic pathway
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In enzymology, a dihydroxyphenylalanine ammonia-lyase (EC 4.3.1.11, entry deleted) is a non-existing enzyme that catalyzes the chemical reaction

3,4-dihydroxy-L-phenylalanine trans-caffeate + NH3

Hence, this enzyme has one substrate, 3,4-dihydroxy-L-phenylalanine (L-DOPA), and two products, trans-caffeate and NH3.

This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is 3,4-dihydroxy-L-phenylalanine ammonia-lyase (trans-caffeate-forming). Other names in common use include beta-(3,4-dihydroxyphenyl)-L-alanine (DOPA) ammonia-lyase, and 3,4-dihydroxy-L-phenylalanine ammonia-lyase. This enzyme participates in tyrosine metabolism.

Related Research Articles

<span class="mw-page-title-main">Tyrosine</span> Amino acid

L-Tyrosine or tyrosine or 4-hydroxyphenylalanine is one of the 20 standard amino acids that are used by cells to synthesize proteins. It is a non-essential amino acid with a polar side group. The word "tyrosine" is from the Greek tyrós, meaning cheese, as it was first discovered in 1846 by German chemist Justus von Liebig in the protein casein from cheese. It is called tyrosyl when referred to as a functional group or side chain. While tyrosine is generally classified as a hydrophobic amino acid, it is more hydrophilic than phenylalanine. It is encoded by the codons UAC and UAU in messenger RNA.

<small>L</small>-DOPA Chemical compound

l-DOPA, also known as levodopa and l-3,4-dihydroxyphenylalanine, is an amino acid that is made and used as part of the normal biology of some plants and animals, including humans. Humans, as well as a portion of the other animals that utilize l-DOPA, make it via biosynthesis from the amino acid l-tyrosine. l-DOPA is the precursor to the neurotransmitters dopamine, norepinephrine (noradrenaline), and epinephrine (adrenaline), which are collectively known as catecholamines. Furthermore, l-DOPA itself mediates neurotrophic factor release by the brain and CNS. l-DOPA can be manufactured and in its pure form is sold as a psychoactive drug with the INN levodopa; trade names include Sinemet, Pharmacopa, Atamet, and Stalevo. As a drug, it is used in the clinical treatment of Parkinson's disease and dopamine-responsive dystonia.

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

Caffeic acid is an organic compound that is classified as a hydroxycinnamic acid. This yellow solid consists of both phenolic and acrylic functional groups. It is found in all plants because it is an intermediate in the biosynthesis of lignin, one of the principal components of woody plant biomass and its residues.

In enzymology, a caffeate O-methyltransferase is an enzyme that catalyzes the chemical reaction

Caffeate 3,4-dioxygenase (EC 1.13.11.22) is an enzyme that catalyzes the chemical reaction

In enzymology, a stizolobate synthase (EC 1.13.11.29) is an enzyme that catalyzes the chemical reaction

In enzymology, a stizolobinate synthase (EC 1.13.11.30) is an enzyme that catalyzes the chemical reaction

The enzyme 3-aminobutyryl-CoA ammonia-lyase (EC 4.3.1.14) catalyzes the chemical reaction

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

The enzyme aspartate ammonia-lyase (EC 4.3.1.1) catalyzes the chemical reaction

The enzyme carbamoyl-serine ammonia-lyase (EC 4.3.1.13) 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">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:

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

The biosynthesis of phenylpropanoids involves a number of enzymes.

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

Tyrosine ammonia lyase (EC 4.3.1.23, L-tyrosine ammonia-lyase, TAL or Tyrase) is an enzyme in the natural phenols biosynthesis pathway. It transforms L-tyrosine into p-coumaric acid.

3,4-dihydroxyphenylalanine oxidative deaminase (EC 1.13.12.15, 3,4-dihydroxy-L-phenylalanine: oxidative deaminase, oxidative deaminase, DOPA oxidative deaminase, DOPAODA) is an enzyme with systematic name 3,4-dihydroxy-L-phenylalanine:oxygen oxidoreductase (deaminating). This enzyme catalyses the following chemical reaction

The enzyme 3,4-dihydroxyphenylalanine reductive deaminase (EC 4.3.1.22, reductive deaminase, DOPA-reductive deaminase, DOPARDA; systematic name 3,4-dihydroxy-L-phenylalanine ammonia-lyase (3,4-dihydroxyphenylpropanoate-forming)) catalyses the following chemical reaction

Phenylalanine/tyrosine ammonia-lyase (EC 4.3.1.25, PTAL, bifunctional PAL) is an enzyme with systematic name L-phenylalanine(or L-tyrosine):trans-cinnamate(or trans-p-hydroxycinnamate) ammonia-lyase. This enzyme catalyses the following chemical reaction

References