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DL-o-Tyrosine Sale

(Synonyms: DL-O-络氨酸,NSC 72345; Ortho-tyrosine; o-DL-Tyrosine; o-Tyrosine) 目录号 : GC49081

A phenylalanine hydroxylation product

DL-o-Tyrosine Chemical Structure

Cas No.:2370-61-8

规格 价格 库存 购买数量
100 mg
¥1,010.00
现货
250 mg
¥1,525.00
现货
500 mg
¥2,021.00
现货

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Sample solution is provided at 25 µL, 10mM.

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产品描述

DL-o-Tyrosine is a hydroxylation product of phenylalanine.1 It is formed from phenylalanine by hydroxyl radicals generated during radiolysis and can be further hydroxylated to form 2,3-dihydroxyphenylalanine (2,3-DOPA). DL-o-Tyrosine has been used as a marker of irradiation processing in poultry meat.2

1.?egota, H., Ko?odziejczyk, K., KrÓl, M., et al.o-Tyrosine hydroxylation by OH

Chemical Properties

Cas No. 2370-61-8 SDF
别名 DL-O-络氨酸,NSC 72345; Ortho-tyrosine; o-DL-Tyrosine; o-Tyrosine
Canonical SMILES O=C(C(CC1=C(O)C=CC=C1)N)O
分子式 C9H11NO3 分子量 181.2
溶解度 H2O : 5 mg/mL (27.60 mM; ultrasonic and warming and heat to 60°C); DMSO : 2 mg/mL (11.04 mM; Need ultrasonic) 储存条件 -20°C
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1 mg 5 mg 10 mg
1 mM 5.5188 mL 27.5938 mL 55.1876 mL
5 mM 1.1038 mL 5.5188 mL 11.0375 mL
10 mM 0.5519 mL 2.7594 mL 5.5188 mL
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Research Update

Oxidation and oxygenation of L-amino acids catalyzed by a L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501

J Biochem 1984 Aug;96(2):421-7.PMID:6501250DOI:10.1093/oxfordjournals.jbchem.a134853.

A number of L-amino acids and derivatives were tested as substrates for the purified Pseudomonas L-phenylalanine oxidase. The reaction products of these amino acids were analyzed by high performance liquid chromatography and the kinetic properties of the reactions were partially characterized. In addition to L-phenylalanine, L-tyrosine, DL-o-Tyrosine, DL-m-tyrosine, p-fluoro-DL-phenylalanine and beta-2-thienyl-DL-alanine served as substrates for both oxidation and oxygenation catalyzed by the enzyme. On the other hand, L-methionine and L-norleucine were enzymically converted to the corresponding alpha-keto acids with the consumption of oxygen and with the formation of ammonia and hydrogen peroxide in stoichiometric amounts. Kinetic studies showed that the Km values for oxidation and oxygenation of L-phenylalanine by the enzyme were 2.04 mM and 1.96 mM for oxygen, and 13.3 microM and 11.1 microM for L-phenylalanine, respectively. omega-Phenyl fatty acids such as phenylacetic acid, 3-phenylpropionic acid and 4-phenylbutyric acid were competitive inhibitors of the enzyme towards L-phenylalanine. Both oxidation and oxygenation of L-phenylalanine by the enzyme were also inhibited by phenylacetic acid competitively.

Mechanisms underlying the effects of 5-hydroxytryptamine and 5-hydroxytryptophan in pancreatic islets. A proposed role for L-aromatic amino acid decarboxylase

Endocrinology 1983 Apr;112(4):1524-9.PMID:6339207DOI:10.1210/endo-112-4-1524.

Microdissected pancreatic islets of noninbred ob/ob mice were used in studies of 5-hydroxytryptamine (5-HT) and 5-hydroxytryptophan (5-HTP) effects on insulin release. The potentiating effect of 4 mM L-5-HTP on glucose-induced insulin release was inhibited by the decarboxylase inhibitors benserazide (100 microM), alpha-monofluoromethyldopa (10 or 100 microM), carbidopa (50 or 500 microM), and NSD 1015 (5 or 50 microM). Activation of L-aromatic amino acid decarboxylase by DL-m-tyrosine (4 mM) or DL-o-Tyrosine (4 mM) potentiated glucose-induced insulin release, whereas L-dopa (4 mM) inhibited it. Glucose oxidation was unaffected by L-5-HTP but slightly stimulated by 5-HT. Glucose-induced efflux of 33Pi was reduced by 5-HT but not affected by 5-HTP. These results are compatible with the ideas that 5-HT inhibits glucose-induced insulin release by affecting early steps in the beta-cell stimulus-secretion coupling and that 5-HTP-potentiation of insulin release is probably mediated by the decarboxylase activity but is independent of the 5-HT formed.