Pyrazolylalanine synthase

Last updated
pyrazolylalanine synthase
Identifiers
EC no. 4.2.1.50
CAS no. 37290-81-6
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

The enzyme pyrazolylalanine synthase (EC 4.2.1.50) catalyzes the chemical reaction

L-serine + pyrazole 3-(pyrazol-1-yl)-L-alanine + 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 L-serine hydro-lyase [adding pyrazole 3-(pyrazol-1-yl)-L-alanine-forming]. Other names in common use include β-pyrazolylalaninase, β-(1-pyrazolyl)alanine synthase, and L-serine hydro-lyase (adding pyrazole). It employs one cofactor, pyridoxal phosphate.

Related Research Articles

<span class="mw-page-title-main">Pyridoxal phosphate</span> Active form of vitamin B6

Pyridoxal phosphate (PLP, pyridoxal 5'-phosphate, P5P), the active form of vitamin B6, is a coenzyme in a variety of enzymatic reactions. The International Union of Biochemistry and Molecular Biology has catalogued more than 140 PLP-dependent activities, corresponding to ~4% of all classified activities. The versatility of PLP arises from its ability to covalently bind the substrate, and then to act as an electrophilic catalyst, thereby stabilizing different types of carbanionic reaction intermediates.

<span class="mw-page-title-main">Amino acid synthesis</span> The set of biochemical processes by which amino acids are produced

Amino acid synthesis is the set of biochemical processes by which the amino acids are produced. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesize all amino acids. For example, humans can synthesize 11 of the 20 standard amino acids. These 11 are called the non-essential amino acids).

<span class="mw-page-title-main">Cystathionine beta synthase</span> Mammalian protein found in humans

Cystathionine-β-synthase, also known as CBS, is an enzyme (EC 4.2.1.22) that in humans is encoded by the CBS gene. It catalyzes the first step of the transsulfuration pathway, from homocysteine to cystathionine:

<span class="mw-page-title-main">Transsulfuration pathway</span>

The transsulfuration pathway is a metabolic pathway involving the interconversion of cysteine and homocysteine through the intermediate cystathionine. Two transsulfurylation pathways are known: the forward and the reverse.

The enzyme L-3-cyanoalanine synthase catalyzes the chemical reaction

The enzyme S-carboxymethylcysteine synthase catalyzes the reaction

The enzyme ectoine synthase (EC ) catalyzes the chemical reaction

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

The enzyme imidazoleglycerol-phosphate dehydratase (EC 4.2.1.19) catalyzes the chemical reaction

The enzyme isohexenylglutaconyl-CoA hydratase (EC 4.2.1.57) catalyzes the chemical reaction

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

The enzyme threonine synthase (EC 4.2.3.1) catalyzes the chemical reaction

In enzymology, a beta-pyrazolylalanine synthase (EC 2.5.1.51) is an enzyme that catalyzes the chemical reaction

In enzymology, a cysteine synthase is an enzyme that catalyzes the chemical reaction

In enzymology, a L-mimosine synthase (EC 2.5.1.52) is an enzyme that catalyzes the chemical reaction

In enzymology, an uracilylalanine synthase (EC 2.5.1.53) is an enzyme that catalyzes the chemical reaction

In enzymology, a zeatin 9-aminocarboxyethyltransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Cys/Met metabolism PLP-dependent enzyme family</span>

In molecular biology, the Cys/Met metabolism PLP-dependent enzyme family is a family of proteins including enzymes involved in cysteine and methionine metabolism which use PLP (pyridoxal-5'-phosphate) as a cofactor.

Tryptophan synthase (indole-salvaging) (EC 4.2.1.122, tryptophan synthase beta2) is an enzyme with systematic name L-serine hydro-lyase (adding indole, L-tryptophan-forming). This enzyme catalyses the following 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

References