6042-04-2

Usage

Chemical Properties

Light yellow crystalline powder

InChI:InChI=1/C11H15N3O3S/c1-18-7-6-10(12)11(15)13-8-2-4-9(5-3-8)14(16)17/h2-5,10H,6-7,12H2,1H3,(H,13,15)/t10-/m0/s1

Upstream product

• 70968-22-8 Boc-Met-pNA 
• 2488-15-5 N-tert-butoxycarbonyl-L-methionine 
• 100-01-6 4-nitro-aniline 
• 84890-95-9 C₁₅H₂₇NO₆S 

Downstream Products

• 15080-84-9 Phe-Met 
• 63-68-3 L-methionine 
• 85697-95-6 H-Tyr-Leu-Met-pNA*HCl 
• 82155-57-5 Suc-Tyr-Leu-Met-pNA 
• 85697-86-5 Boc-Tyr-Leu-Met-pNA 
• 85698-08-4 H-Leu-Met-pNA*HCl 
• 100-01-6 4-nitro-aniline 

Relevant academic research and scientific papers

Characterisation of the aminopeptidase from non-germinated winter rape (Brassica napus L.) seeds

Rapeseed plays a crucial role in food and fuel industry. Since aminopeptidases take part in many physiological processes in all organisms, it is important to learn their role and characteristics in economically relevant plants. Extracts of non-germinated winter rape seeds were screened for aminopeptidase activity. Substrate specificity, the influence of pH and temperature, as well as effect of protease inhibitors and chosen metal ions on the aminopeptidase activity were determined. The approximate molecular weight estimated by NATIVE-PAGE and SDS-PAGE electrophoresis was ～60 kDa. The partially purified enzyme as well as the aminopeptidases present in crude extract cleaved preferentially Phe-pNA. The activity profiles toward several substrates were also determined. Maximum activity was observed at pH 6.5 and temperature of 40 °C for Phe-pNA as a substrate. Two visible picks in the pH profile toward Phe-pNA, together with other results (IEF) suggest the presence of more than one aminopeptidase, having similar molecular mass. Much lower activity and broad pH profiles were observed for Leu- and Ala-pNA as substrates.

Methionine analogues as inhibitors of methionyl-tRNA synthetase

A series of methionine analogues have been synthesized as inhibitors of methionyl-tRNA synthetase and evaluated for their inhibitory activities of E. coli methionyl-tRNA synthetase and bacterial growth. Among them, L-methionine hydroxamate 20 has proved to be the best inhibitor of the enzyme with K(i) = 19 μM and showed a growth inhibition against E. coli JM 109, P. vulganis 6059 and C. freundii 8090.