70671-54-4

Usage

Chemical Properties

White crystalline

InChI:InChI=1/C14H20N2O4/c15-9-5-4-8-12(13(17)18)16-14(19)20-10-11-6-2-1-3-7-11/h1-3,6-7,12H,4-5,8-10,15H2,(H,16,19)(H,17,18)/t12-/m1/s1

Upstream product

• 87797-02-2 benzyloxycarbonyl-lysine 
• 501-53-1 benzyl chloroformate 
• 7274-88-6 D-lysine hydrochloride 

Downstream Products

• 188625-18-5 (R)-6-Amino-2-benzyloxycarbonylamino-hexanoic acid methyl ester 
• 284469-94-9 C₁₈H₂₆N₂O₅ 
• 867150-38-7 Nα-Z-D-aminoadipic acid-δ-semialdehyde 
• 108491-55-0 D-Z-α-amino-ε-caprolactam 
• 174658-19-6 (R)-2-Benzyloxycarbonylamino-6-tert-butoxycarbonylamino-hexanoic acid 4-nitro-benzyl ester 

Relevant academic research and scientific papers

Stereocontrolled synthesis of onchidins

(Chemical Equation Presented) The first total synthesis of a molecule possessing the stereochemistry proposed for onchidin is described. The structure synthesized appears to be different from that of the marine natural product.

Enantioselective Enzymatic Cleavage of N-Benzyloxycarbonyl Groups

A new enzymatic process for the enantioselective cleavage of N-benzyloxycarbonyl (Cbz) groups from protected amino acids and related compounds has been developed. The Cbz-deprotecting enzyme was isolated from cell extracts of Sphingomonas paucimobilis SC 16113 and purified to homogeneity. The purified protein has a molecular weight of 155,000 daltons and a subunit size of 44,000 daltons.

Fairly marked enantioselectivity for the hydrolysis of amino acid esters by chemically modified enzymes

The hydrolysis (deacylation) of enantiomeric substrates by the chemically modified enzymes decanoyl-α-chymotrypsin and decanoyl-trypsin was studied. Reaction activity for decanoyl-α-chymotrypsin was lower than that for the native enzyme, although intriguingly the enantioselectivity was markedly enhanced as compared with the native enzyme. In particular, the apparently complete enantioselective catalysis was attained for the hydrolytic cleavage of p-nitrophenyl N-dodecanoyl- D(L)-phenylalaninates. The enhancement of enantioselectivity, however, was not observed for decanoyl-trypsin. These results suggest that the chemically modified α-chymotrypsin by addition of hydrophobic groups has promoted enantioselectivity for the hydrolysis of hydrophobic esters.