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Merck
CN

T3754

L-Tyrosine

≥98% (HPLC)

Synonym(s):

(S)-2-Amino-3-(4-hydroxyphenyl)propionic acid, 3-(4-Hydroxyphenyl)-L-alanine

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About This Item

Linear Formula:
4-(HO)C6H4CH2CH(NH2)CO2H
CAS Number:
Molecular Weight:
181.19
NACRES:
NA.26
PubChem Substance ID:
eCl@ss:
32160406
UNSPSC Code:
12352209
EC Number:
200-460-4
MDL number:
Beilstein/REAXYS Number:
392441
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Product Name

L-Tyrosine, reagent grade, ≥98% (HPLC)

InChI key

OUYCCCASQSFEME-QMMMGPOBSA-N

InChI

1S/C9H11NO3/c10-8(9(12)13)5-6-1-3-7(11)4-2-6/h1-4,8,11H,5,10H2,(H,12,13)/t8-/m0/s1

SMILES string

N[C@@H](Cc1ccc(O)cc1)C(O)=O

grade

reagent grade

assay

≥98% (HPLC)

form

powder

color

white to off-white

mp

>300 °C (dec.) (lit.)

solubility

1 M HCl: soluble 50 mg/mL

application(s)

detection

Quality Level

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Application

L-Tyrosine has been used to prepare tyrosine solution for tyrosinase assay. It has also been used to assay pepsin activity.

Biochem/physiol Actions

L-Tyrosine is a non-essential amino acid with a polar side chain. It is utilized by cells to synthesize proteins that have a role in signal transduction. L-Tyrosine is a proteogenic amino acid that acts as a receiver of phosphate groups that are transferred by kinases.

Other Notes

Amino acid precursor of dopamine and other catecholamines

Storage Class

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Gloves


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Study of Physiochemical Parameters for Optimizing Tyrosinase Activity in Rhodococcus ruber C4 and Pseudomonas geniculata C7/C10
Sapna S. Ingle
Journal of Pharmacy Research, 9(6) (2015)
Karen Timberlake
Chemistry, An Introduction to General, Organic, and Biological Chemistry (2016)
Effect of insoluble fiber supplementation applied at different ages on digestive organ weight and digestive enzymes of layer-strain poultry
J. S. Yokhana
Poultry Science, 95(3), 550-559 (2016)
John W Hill
Chemistry for Changing Times (2016)
Keisuke Saito et al.
Proceedings of the National Academy of Sciences of the United States of America, 110(19), 7690-7695 (2013-04-20)
Using quantum mechanics/molecular mechanics calculations and the 1.9-Å crystal structure of Photosystem II [Umena Y, Kawakami K, Shen J-R, Kamiya N (2011) Nature 473(7345):55-60], we investigated the H-bonding environment of the redox-active tyrosine D (TyrD) and obtained insights that help

Protocols

Proteinase K activity measured via spectrophotometry using hemoglobin substrate, crucial for enzyme characterization.

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