N-Cbz-L-tyrosine (BAT-003383)
* For research use only

N-Cbz-L-tyrosine is an N-Cbz-protected form of L-Tyrosine.

Category
CBZ-Amino Acids
Catalog number
BAT-003383
CAS number
1164-16-5
Molecular Formula
C17H17NO5
Molecular Weight
315.30
N-Cbz-L-tyrosine
IUPAC Name
(2S)-3-(4-hydroxyphenyl)-2-(phenylmethoxycarbonylamino)propanoic acid
Synonyms
N-[(Phenylmethoxy)carbonyl]-L-tyrosine; N-Carboxy-L-tyrosine N-Benzyl Ester; (Benzyloxycarbonyl)tyrosine; Benzyloxycarbonyl-L-tyrosine; Carbobenzoxy-L-tyrosine; Carbobenzoxytyrosine; L-(Carbobenzyloxy)tyrosine; N-(Benzyloxycarbonyl)-L-tyrosine; N-(Benzyloxycarbonyl)tyrosine; N-Carbobenzoxy-L-tyrosine; N-Carbobenzoxytyrosine; N-Carbobenzyloxy-L-tyrosine; NSC 88488; Z-L-tyrosine
Appearance
Off-white Solid
Purity
≥98% by HPLC
Density
1.1781 g/cm3
Melting Point
94-98°C
Boiling Point
570.8°C
Storage
-20°C
Solubility
Soluble in Acetic Acid (Sparingly), DMSO (Slightly), Methanol (Sparingly)
InChI
InChI=1S/C17H17NO5/c19-14-8-6-12(7-9-14)10-15(16(20)21)18-17(22)23-11-13-4-2-1-3-5-13/h1-9,15,19H,10-11H2,(H,18,22)(H,20,21)/t15-/m0/s1
InChI Key
MCRMUCXATQAAMN-HNNXBMFYSA-N
Canonical SMILES
C1=CC=C(C=C1)COC(=O)NC(CC2=CC=C(C=C2)O)C(=O)O
1.Detection of a water molecule in the active-site of bacteriorhodopsin: hydrogen bonding changes during the primary photoreaction.
Fischer WB1, Sonar S, Marti T, Khorana HG, Rothschild KJ. Biochemistry. 1994 Nov 1;33(43):12757-62.
FTIR-difference spectroscopy in combination with site-directed mutagenesis has been used to investigate the role of water during the photocycle of bacteriorhodopsin. At least one water molecule is detected which undergoes an increase in H-bonding during the primary bR-->K phototransition. Bands due to water appear in the OH stretch region of the bR-->K FTIR-difference spectrum which downshift by approximately 12 cm-1 when the sample is hydrated with H2(18)O. In contrast to 2H2O, the H2(18)O-induced shift is not complete, even after 24 h of hydration. This indicates that even though water is still able to exchange protons with the outside medium, it is partially trapped in the interior of the protein. In the mutant Y57D, these bands are absent while a new set of bands appear at much lower frequencies which undergo H2(18)O-induced shifts. It is concluded that the water molecule we detect is located inside the bR active-site and may interact with Tyr-57.
2.Interaction of vanadyl (VO2+) with ligands containing serine, tyrosine, and threonine.
Ebel M1, Rehder D. Inorg Chem. 2006 Sep 4;45(18):7083-90.
Reaction of vanadyl sulfate with an aldehyde (2-hydroxy-1-naphthaldehyde (nap); 3-methoxysalicylaldehyde = o-vanillin (van)) and an amino acid carrying an OH group (L-tyrosine (L-tyr); L-serine (L-ser), L-threonine (L-thr)) yielded the complexes [VO(nap-D-Tyr)(H2O)] 1a, [VO(van-D,L-Tyr)(H2O)] 1c, [VO(nap-Ser)(H2O)] 2a, [VO(van-D,L-Ser)(H2O)] 2b, [VO(nap-Thr)(H2O)] 3a, and [VO(van-Thr)(H2O)] 3b. [VO(nap-L-tyr(H2O)], 1b, was obtained from the reaction between [VO(nap)(2)] and l-TyrOMe. The crystal and molecular structures of 1a.CH3OH, 1b.CH3OH, 1c.H2O, 2b.2H2O, and the Schiff base nap-D,L-TyrOMe (4) are reported. The ligands coordinate in a tridentate manner through the phenolate component of nap or van, the imine nitrogen, and the carboxylate of the amino acid. Direct coordination of the (deprotonated) OH amino acid functionality is not observed in these complexes. Instead, the OH groups are involved in hydrogen bonding, leading, along with pi-pi stacking, to extended one- and three-dimensional supramolecular networks.
Bio Calculators
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Concentration (start) x Volume (start) = Concentration (final) x Volume (final)
It is commonly abbreviated as: C1V1 = C2V2

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Tip: Chemical formula is case sensitive. C22H30N4O c22h30n40
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