174843-67-5

Upstream product

• 4896-75-7 <2-2H2>glycine 
• 501-53-1 benzyl chloroformate 

Downstream Products

• 84712-45-8 C₁₆H₁₂⁽²⁾H₂N₂O₆ 
• 188881-28-9 C₁₉H₁₇⁽²⁾H₂N₃O₇ 
• 1158245-93-2 Z-Gly-2,2-d2-L-Phe-STmob 

Relevant academic research and scientific papers

Vibrational spectra of N-acetylglycine oligomers. Part 2. - Raman scattering study of selectively C-deuteriated oligomers with polyglycine I- and II-type structures

Selectively C-deuteriated N-acetylglycine trimer and tetramer acid types have been synthesized, and their two crystalline modifications, solid-A and solid-B [which correspond in structure to polyglycine (PG) II and I, respectively] have been prepared. Raman scattering spectra have been measured for a series of these glycine oligomers, and the CH2- and CD2-characteristic modes have been investigated in detail. Assignment of the CH2-characteristic bands to each CH2 group in the oligomers has been carried out successfully. In particular, the results obtained from the CD2 stretch region show that N- and C-terminal glycine residues for the PGI- and PGII-type trimers and tetramers are all in very similar environments and that the glycine residues which are sandwiched between the two terminal residues are also in a similar environment for both the trimers and the tetramers.

Correlative Variations in Enzyme-Derived and Substrate-Derived Structures of Catalytic Transition States. Implications for the Catalytic Strategy of Acyl-Transfer Enzymes

Acetylchymotrypsin, acetyl elastase and (carbobenzyloxy)glycyl elastase all undergo hydrolysis with the same overall solvent isotope effect, which arises from a single protonic site n/k1 = 2.45(1-n + n/2.45)>. chymotrypsin, however, shows a larger effect arising from at least two sites n/k1 = 3.34(1-n + n/1.85)2>.Formylchymotrypsin and acetylchymotrypsin undergo deacylation with α-deuterium and β-deuteium secondary isotope effects, respectively, that suggest fractional tetrahedral character at the transition state of about 0.44 (vs. 0.58 - 0.66 for similar nonenzymic reactions) when compared to equilibrium isotope effects for complete addition.The effect for acetyl elastase suggests much less tetrahedral character (0.27).Addition of an N-acyl function leads to a more inverse isotope effect, per deuterium, and thus to an apparent increase in tetrahedral character: to 0.84 for chymotrypsin; to 0.43 for (carbobenzyloxy)glycyl elastase.It is concluded that enzyme-substrate interactions at the transition state can alter both enzyme structure, as shown by the solvent isotope effects, and substrate structure as shown by the substrate isotope effects.Such alterations, in the combination of enzyme with natural substrate, probably adjust both structures for optimal catalytic interaction.