1676-77-3

Basic information

• Product Name: Glycine, N-[N-[(phenylmethoxy)carbonyl]-L-seryl]-, methyl ester
• CAS NO: 1676-77-3
• Molecular Formula: C14H18N2O6
• Molecular Weight: 310.307
• Mol File: 1676-77-3.mol
• Article Data: 3

Chemical Properties

• CAS DataBase Reference: Glycine, N-[N-[(phenylmethoxy)carbonyl]-L-seryl]-, methyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: Glycine, N-[N-[(phenylmethoxy)carbonyl]-L-seryl]-, methyl ester(1676-77-3)
• EPA Substance Registry System: Glycine, N-[N-[(phenylmethoxy)carbonyl]-L-seryl]-, methyl ester(1676-77-3)

Safety Data

• Hazardous Substances Data: 1676-77-3(Hazardous Substances Data)

Upstream product

• 41446-15-5 Z-Ser-N3 
• 616-34-2 methoxycarbonylmethylamine 
• 2768-56-1 Z-DL-serine 
• 26582-86-5 benzyl (1S)-2-hydrazino-1-(hydroxymethyl)-2-oxoethylcarbamate 
• 1145-80-8 N-(benzyloxycarbonyl)-L-serine 

Downstream Products

• 1738-94-9 N-[N-(N-benzyloxycarbonyl-L-seryl)-glycyl]-glycine benzyl ester 
• 95930-68-0 N-benzyloxycarbonyl-N'-methoxycarbonylmethyloxamide 
• 621-84-1 O-benzyl carbamate 
• 95930-67-9 N-benzyloxycarbonyl-O-<2-benzyloxycarbonylamino-N-(methoxycarbonylmethyl)malonamoyl>serylglycine methyl ester 

Relevant articles and documents

Zinc-catalyzed amide cleavage and esterification of β- hydroxyethylamides

Snipping tool: Zn(OTf)2 is an efficient catalyst for selective cleavage of amides bearing a β-hydroxyethyl group on the nitrogen atom. The mechanism involves an N,O-acyl rearrangement and transesterification. This new catalytic system can be applied to sequence-specific peptide bond scission at the amine side of a serine residue. Tf=trifluoromethanesulfonyl. Copyright

Protein backbone modification by novel C(α)-C side-chain scission

α-Ketoamide (-NH-CO-CO-) units in intact peptides are generated from Ser/Thr residues via Ru(VIII)-catalyzed C(α)-C side-chain scission. Facets associated with this novel α-carbon modification have been probed with 75 peptides chosen to represent every possible peptide environment. The reactions were carried out at room temperature with in situ generated Ru(VIII) in biphasic (CH3CN/CCl4/pH 3 phosphate buffer, 1:1:2 v/v) medium. Whereas Ser/Thr residues placed at the C-terminal end in peptides undergo N-C bond scission leading to des-Ser/Thr peptide amides - thus acting as Gly equivalents in simulating the α-amidating action of pituitary enzymes - those located at the N-terminal or nonterminal or even at the C-terminal position (protected as amide) were found to undergo oxidative C-C bond scission (involving C(α) and C side-chain bond), resulting in the generation of α-ketoamide (-NH-CO-CO-) units in the intact peptide backbone. The difference in the products arising from C(α)-C side-chain scission of Ser/Thr esters and amides is rationalized on the basis of a common mechanism involving either oxaloesters [PeP-NH-CO-COX; X = OMe] or oxalamides [X = NH2 or NH-Pep] arising from the oxidation of initially formed carbinolamide intermediates [Pep-NH-CH(OH)-COX], wherein, while the former are shown to undergo hydrolysis to terminal amides [Pep-NH2], the oxalamides are found to be stable to hydrolysis. Ancillary noteworthy findings are those of peptide bond scission when contiguous Ser-Ser/Thr-Thr residues are present and the oxidative cleavage at C-terminal Tyr/Trp sites generating des amides. The oxidative methodology presented here is mild, simple, and practical and proceeds with chiral retention. The insensitivity of a large number of amino acid residues, such as Gly, Ala, Leu, Asn, Gln, Asp, Glu, Pro, Arg, Phe, Lys, Val, and Aib, and N-protecting groups, such as Boc, Z, and Bz, toward Ru(VIII) under the experimental conditions should make this methodology practical and useful. Sulfur-containing amino acids Cys and Met get oxidized to sulfones in the products.