Z-O-benzyl-L-serine
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Z-O-benzyl-L-serine

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Category
CBZ-Amino Acids
Catalog number
BAT-003402
CAS number
20806-43-3
Molecular Formula
C18H19NO5
Molecular Weight
329.40
Z-O-benzyl-L-serine
IUPAC Name
(2S)-3-phenylmethoxy-2-(phenylmethoxycarbonylamino)propanoic acid
Synonyms
Z-L-Ser(Bzl)-OH; (2S)-3-phenylmethoxy-2-(phenylmethoxycarbonylamino)propanoic acid; CBZ-SER(BZL)-OH; N-[(phenylmethoxy)carbonyl]-O-(phenylmethyl)-L-serine; Cbz-Ser(Bzl)-OH; Z-Ser(Bzl)-OH; (S)-3-(benzyloxy)-2-(benzyloxycarbonylamino)propanoic acid; O-benzyl-N-benzyloxycarbonyl-L-serine
Appearance
White powder
Purity
≥ 98.5% (HPLC)
Density
1.253±0.060 g/cm3
Melting Point
91-99 °C
Boiling Point
537.1±50.0 °C
Storage
Store at 2-8 °C
InChI
InChI=1S/C18H19NO5/c20-17(21)16(13-23-11-14-7-3-1-4-8-14)19-18(22)24-12-15-9-5-2-6-10-15/h1-10,16H,11-13H2,(H,19,22)(H,20,21)/t16-/m0/s1
InChI Key
CYYRLHUAMWRBHC-INIZCTEOSA-N
Canonical SMILES
C1=CC=C(C=C1)COCC(C(=O)O)NC(=O)OCC2=CC=CC=C2
1. N-Heterocyclic Carbene-Catalyzed Random Copolymerization of N-Carboxyanhydrides of α-Amino Acids
Kuen Hee Eom, Seokhyeon Baek, Il Kim Polymers (Basel). 2021 Oct 25;13(21):3674. doi: 10.3390/polym13213674.
Synthetic polypeptides prepared from N-carboxyanhydrides (NCAs) of α-amino acids are useful for elucidating the relationship between the primary structure of natural peptides and their immunogenicity. In this study, complex copolypeptide sequences were prepared using a recently developed technique; specifically, the random copolymerization of l-alanine NCA with NCAs of l-glutamic acid 5-benzylester (Bn-Glu NCA), S-benzyl-cysteine (Bn-Cys NCA), O-benzyl-l-serine (Bn-Ser NCA), and l-phenylalanine (Phe NCA) was performed using N-heterocyclic carbene (NHC) catalysts. The NHC-initiated Ala NCA/Bn-Glu NCA and Ala NCA/Bn-Cys NCA copolymerization reactions achieved 90% conversion within 30 min. The reactivity ratio values estimated using the Kelen and Tüdos method show that poly(Bn-Glu-co-Ala) and poly(Bn-Cys-co-Ala) have random repeating units with rich alternating sequences, whereas poly(Bn-Ser-co-Ala) and poly(Phe-co-Ala) contain a larger proportion of Ala-repeating units than Bn-Ser and Phe in random placement.
2. Reactions of O-acyl-L-serines with tryptophanase, tyrosine phenol-lyase, and tryptophan synthase
R S Phillips Arch Biochem Biophys. 1987 Jul;256(1):302-10. doi: 10.1016/0003-9861(87)90450-4.
The reactions of tryptophanase, tyrosine phenol-lyase, and tryptophan synthase with a new class of substrates, the O-acyl-L-serines, have been examined. A method for preparation of O-benzoyl-L-serine in high yield from tert.-butyloxycarbonyl (tBoc)-L-serine has been developed. Reaction of the cesium salt of tBoc-L-serine with benzyl bromide in dimethylformamide gives tBoc-L-serine benzyl ester in excellent yield. Acylation with benzoyl chloride and triethylamine in acetonitrile followed by hydrogenolysis with 10% palladium on carbon in trifluoroacetic acid gives O-benzoyl-L-serine, isolated as the hydrochloride salt. O-Benzoyl-L-serine is a good substrate for beta-elimination or beta-substitution reactions catalyzed by both tryptophanase and tyrosine phenol-lyase, with Vmax values 5- to 6-fold those of the physiological substrates and comparable to that of S-(o-nitrophenyl)-L-cysteine. Unexpectedly, O-acetyl-L-serine is a very poor substrate for these enzymes, with Vmax values about 5% of those of the physiological substrates. Both O-acyl-L-serines are poor substrates for tryptophan synthase, measured either by the synthesis of 5-fluoro-L-tryptophan from 5-fluoroindole and L-serine catalyzed by the intact alpha 2 beta 2 subunit or by the beta-elimination reaction catalyzed by the isolated beta 2 subunit. With all three enzymes, the elimination of benzoate appears to be irreversible. These results suggest that the binding energy from the aromatic ring of O-benzoyl-L-serine is used to lower the transition-state barrier for the elimination reactions catalyzed by tryptophanase and tyrosine phenol-lyase. Our findings support the suggestion (M. N. Kazarinoff and E. E. Snell (1980) J. Biol. Chem. 255, 6228-6233) that tryptophanase undergoes a conformational change during catalysis and suggest that tyrosine phenol-lyase also may undergo a conformational change during catalysis.
3. Facile synthesis of N-Fmoc-serine-S-GlcNAc: a potential molecular probe for the functional study of O-GlcNAc
Y Ohnishi, M Ichikawa, Y Ichikawa Bioorg Med Chem Lett. 2000 Jun 5;10(11):1289-91. doi: 10.1016/s0960-894x(00)00223-7.
A metabolically stable beta-N-acetylglucosaminyl-1-thio-N-Fmoc-serine (S-GlcNAc-Ser) derivative was synthesized in two procedures: one involving a coupling of a readily obtainable 1-pseudo-thiourea of GlcNAc (S-GlcNAc) and iodo-N-Boc-L-alanine benzyl ester, and the other utilizing a modified Mitsunobu reaction of GlcNAc-SH and a serine derivative.
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