DL-Tyrosine
(Synonyms: DL-酪氨酸) 目录号 : GC39783
DL-Tyrosine 是由必需氨基酸苯丙氨酸合成的芳香族非必需氨基酸。DL-Tyrosine 是几种重要神经递质（肾上腺素、去甲肾上腺素、多巴胺）的前体。
Cas No.:556-03-6
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >97.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
DL-Tyrosine is an aromatic nonessential amino acid synthesized from the essential amino acid phenylalanine. DL-Tyrosine is a precursor for several important neurotransmitters (epinephrine, norepinephrine, dopamine)[1].
[1]. ClementeBretti, et al. Some thermodynamic properties of dl-Tyrosine and dl-Tryptophan. Effect of the ionic medium, ionic strength and temperature on the solubility and acid-base properties. Fluid Phase Equilibria.
| Cas No. | 556-03-6 | SDF | |
| 别名 | DL-酪氨酸 | ||
| Canonical SMILES | NC(CC1=CC=C(O)C=C1)C(O)=O | ||
| 分子式 | C9H11NO3 | 分子量 | 181.19 |
| 溶解度 | Soluble in DMSO | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 5.5191 mL | 27.5953 mL | 55.1907 mL |
| 5 mM | 1.1038 mL | 5.5191 mL | 11.0381 mL |
| 10 mM | 0.5519 mL | 2.7595 mL | 5.5191 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Racemic resolution of some DL-amino acids using Aspergillus fumigatus L-amino acid oxidase
Curr Microbiol 2011 Jul;63(1):94-9.PMID:21590326DOI:10.1007/s00284-011-9955-8.
The ability of Aspergillus fumigatus L-amino acid oxidase (L-aao) to cause the resolution of racemic mixtures of DL-amino acids was investigated with DL-alanine, DL-phenylalanine, DL-Tyrosine, and DL-aspartic acid. A chiral column, Crownpak CR+ was used for the analysis of the amino acids. The enzyme was able to cause the resolution of the three DL-amino acids resulting in the production of optically pure D-alanine (100% resolution), D-phenylalanine (80.2%), and D-tyrosine (84.1%), respectively. The optically pure D-amino acids have many uses and thus can be exploited industrially. This is the first report of the use of A. fumigatus L: -amino acid oxidase for racemic resolution of DL-amino acids.
Stereospecificity of horseradish peroxidase
Biol Chem 2004 Dec;385(12):1177-84.PMID:15653431DOI:10.1515/BC.2004.152.
We report here on the stereospecificity observed in the action of horseradish peroxidase (HRPC) on monophenol and diphenol substrates. Several enantiomers of monophenols and o-diphenols were assayed: L-tyrosinol, D-tyrosinol, L-tyrosine, DL-Tyrosine, D-tyrosine, L-dopa, DL-dopa, D-dopa, L-alpha-methyldopa, DL-alpha-methyldopa, DL-adrenaline, D-adrenaline, L-isoproterenol, DL-isoproterenol and D-isoproterenol. The electronic density at the carbon atoms in the C-1 and C-2 positions of the benzene ring were determined by NMR assays (delta1 and delta2). This value is related to the nucleophilic power of the oxygen atom of the hydroxyl groups and to its oxidation-reduction capacity. The spatial orientation of the ring substituents resulted in lower Km values for L- than for D-isomers. The kcat values for substrates capable of saturating the enzyme were lower for D- than for L-isomers, although both have the same delta1 and delta2 NMR values for carbons C-1 and C-2, and therefore the same oxidation-reduction potential. In the case of substrates that cannot saturate the enzyme, the values of the binding constant for compound II (an intermediate in the catalytic cycle) followed the order: L-isomer>DL-isomer>D-isomer. Therefore, horseradish peroxidase showed stereospecificity in its affinity toward its substrates (K m) and in their transformation reaction rates (k cat).
Unexpected differences between D- and L- tyrosine lead to chiral enhancement in racemic mixtures
Orig Life Evol Biosph 2002 Aug;32(4):285-97; discussion 283.PMID:12458733DOI:10.1023/a:1020535415283.
We report here an unexpected difference in the solubilities of D- and L-tyrosine in water, which could be discerned by their rate of crystallization and the resulting concentrations of their saturated solutions. A supersaturated solution of 10 mM L-tyrosine at 20 degrees C crystallized much more slowly than that of D-tyrosine under the same conditions, and the saturated solution of L-tyrosine was more concentrated than that of D-tyrosine. Supersaturated solutions of 10 mM DL-Tyrosine in water formed precipitates of predominantly D-tyrosine and DL-Tyrosine, resulting in an excess of L-tyrosine in the saturated solution. The experimental setups were monitored independently by UV-absorption, radioactivity tracing, optical rotation and X-ray diffraction. The process of nucleation and crystallization of D- and L-tyrosine is characterized by an exceptionally high cooperativity. It is possible that minute energy differences between D- and L-tyrosine, originating from parity violation or other non-conservative chiral discriminatory rules, could account for the observations. The physical process that initiated chiral selection in biological systems remains a challenging problem in understanding the origin of life, and it is possible that chiral compounds were concentrated from supersaturated racemic mixtures by preferential crystallization.
THE SOLUBILITIES, APPARENT DISSOCIATION CONSTANTS, AND THERMODYNAMIC DATA OF THE DIHALOGENATED TYROSINE COMPOUNDS
J Gen Physiol 1935 Jul 20;18(6):889-903.PMID:19872898DOI:10.1085/jgp.18.6.889.
1. The solubilities and differential heats of solution of d-tyrosine, DL-Tyrosine, diiodo-dl-tyrosine, dibromo-l-tyrosine (hydrated), dibromo-l-tyrosine (anhydrous), and dichloro-l-tyrosine (hydrated) have been determined. 2. Evidence has been advanced that DL-Tyrosine is a compound. 3. From the solubility determinations at various acidities, the apparent acid and basic dissociation constants of dibromo-l-tyrosine and dichloro-l-tyrosine have been determined at 25 degrees and 40 degrees C. From these data the apparent heats of ionization have been calculated. 4. The question concerning which of the groups in l-tyrosine and its dihalogenated substitution products is responsible for each dissociation constant has been discussed.
Stereospecificity of mushroom tyrosinase immobilized on a chiral and a nonchiral support
J Agric Food Chem 2007 May 30;55(11):4569-75.PMID:17488091DOI:10.1021/jf0701178.
Mushroom tyrosinase was immobilized from an extract onto glass beads covered with the cross-linked totally cinnamoylated derivates of d-sorbitol (sorbitol cinnamate) and glycerine (glycerine cinnamate). The enzyme was immobilized onto the support by direct adsorption, and the quantity of immobilized tyrosinase was higher for sorbitol cinnamate, the support with the higher number of esterified hydroxyls per unit of monosacharide, than for glycerine cinnamate. The results obtained from the stereospecificity study of the monophenolase and diphenolase activity of immobilized mushroom tyrosinase are reported. The enantiomers L-tyrosine, DL-Tyrosine, D-tyrosine, L-dopa, DL-dopa, D-dopa, L-alpha-methyldopa, DL-alpha-methyldopa, L-isoprenaline, DL-isoprenaline, L-adrenaline, DL-adrenaline, L-noradrenaline, and D-noradrenaline were assayed with tyrosinase immobilized on a chiral support (sorbitol cinnamate), whereas L-tyrosine, DL-Tyrosine, D-tyrosine, L-dopa, DL-dopa, D-dopa, L-alpha-methyldopa, and DL-alpha-methyldopa were assayed with tyrosinase immobilized on a nonchiral support (glycerine cinnamate). The same Vmax(app) values for each series of enantiomers were obtained. However, the Km(app) values were different, the l isomers showing lower values than the dl isomers, whereas the highest Km(app) value was obtained with d isomers. No difference was observed in the stereospecificity of tyrosinase immobilized on a chiral (sorbitol cinnamate) or nonchiral (glycerine cinnamate) support.