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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.
Membrane alanyl aminopeptidase also known as alanyl aminopeptidase (AAP) or aminopeptidase N (AP-N) is an enzyme that in humans is encoded by the ANPEP gene.
Catechol 1,2- dioxygenase is an enzyme that catalyzes the oxidative ring cleavage of catechol to form cis,cis-muconic acid:
Aminopeptidases are enzymes that catalyze the cleavage of amino acids from the amino terminus (N-terminus) of proteins or peptides (exopeptidases). They are widely distributed throughout the animal and plant kingdoms and are found in many subcellular organelles, in cytosol, and as membrane components. Aminopeptidases are used in essential cellular functions. Many, but not all, of these peptidases are zinc metalloenzymes.
Tryptophan hydroxylase (TPH) is an enzyme (EC 1.14.16.4) involved in the synthesis of the neurotransmitter serotonin. Tyrosine hydroxylase, phenylalanine hydroxylase, and tryptophan hydroxylase together constitute the family of biopterin-dependent aromatic amino acid hydroxylases. TPH catalyzes the following chemical reaction
Glutamyl aminopeptidase (EC 3.4.11.7, aminopeptidase A, aspartate aminopeptidase, angiotensinase A, glutamyl peptidase, Ca2+-activated glutamate aminopeptidase, membrane aminopeptidase II, antigen BP-1/6C3 of mouse B lymphocytes, L-aspartate aminopeptidase, angiotensinase A2) is an enzyme encoded by the ENPEP gene. Glutamyl aminopeptidase has also recently been designated CD249 (cluster of differentiation 249).
Trichosporon is a genus of anamorphic fungi in the family Trichosporonaceae. All species of Trichosporon are yeasts with no known teleomorphs. Most are typically isolated from soil, but several species occur as a natural part of the skin microbiota of humans and other animals. Proliferation of Trichosporon yeasts in the hair can lead to an unpleasant but non-serious condition known as white piedra. Trichosporon species can also cause severe opportunistic infections (trichosporonosis) in immunocompromised individuals.
In enzymology, a maleylacetate reductase (EC 1.3.1.32) is an enzyme that catalyzes the chemical reaction
In enzymology, a tryptophan alpha,beta-oxidase (EC 1.3.3.10) is an enzyme that catalyzes the chemical reaction
In enzymology, an anthranilate 3-monooxygenase (deaminating) (EC 1.14.13.35) is an enzyme that catalyzes the chemical reaction
In enzymology, a phenol 2-monooxygenase (EC 1.14.13.7) is an enzyme that catalyzes the chemical reaction
In enzymology, a hydroxyquinol 1,2-dioxygenase (EC 1.13.11.37) is an enzyme that catalyzes the chemical reaction
Methionine aminopeptidase 2 is an enzyme that in humans is encoded by the METAP2 gene.
In enzymology, a tryptophan-tRNA ligase is an enzyme that catalyzes the chemical reaction
In enzymology, a tryptophanamidase (EC 3.5.1.57) is an enzyme that catalyzes the chemical reaction
Tryptophanyl-tRNA synthetase, cytoplasmic is an aminoacyl-tRNA synthetase enzyme that attaches the amino acid tryptophan to its cognate tRNA. In humans, it is encoded by the WARS gene.
Tryptophanyl-tRNA synthetase, mitochondrial is an enzyme that in humans is encoded by the WARS2 gene.
Xaa-Trp aminopeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Tryptophan aminopeptidase may refer to:
Amastatin, also known as 3-amino-2-hydroxy-5-methylhexanoyl-L-valyl-L-valyl-L-aspartic acid, is a naturally occurring, competitive and reversible aminopeptidase inhibitor that was isolated from Streptomyces sp. ME 98-M3. It specifically inhibits leucyl aminopeptidase, alanyl aminopeptidase, bacterial leucyl aminopeptidase, leucyl/cystinyl aminopeptidase (oxytocinase/vasopressinase), and, to a lesser extent, glutamyl aminopeptidase, as well as other aminopeptidases. It does not inhibit arginyl aminopeptidase. Amastatin has been found to potentiate the central nervous system effects of oxytocin and vasopressin in vivo. It also inhibits the degradation of met-enkephalin, dynorphin A, and other endogenous peptides.
References
- ↑ Iwayama A, Kimura T, Adachi O, Ameyama M (1983). "Crystallization and characterization of a novel aminopeptidase from Trichosporon cutaneum". Agric. Biol. Chem. 47: 2483–2493. doi: 10.1271/bbb1961.47.2483 .
