2482-25-9Relevant articles and documents
Synthesis of 4-hydroxybenzamides and their salts
Brel,Lisina,Budaeva, Yu. N.,Popov
, p. 2200 - 2202 (2015)
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Substrate Specificity and Stoichiometry of Nα-Benzyloxycarbonyl Amino Acid Urethane Hydrolase from Streptococcus faecalis R ATCC 8043
Matsumura, Eiko,Shin, Takashi,Murao, Sawao,Kawano, Tatsu
, p. 973 - 980 (2007/10/02)
The substrate specificity of a new enzyme, Nα-benzyloxycarbonyl amino acid urethane hydrolase, was investigated.The enzyme hydrolyzed Nα-benzyloxycarbonyl-glycine and -alanine, and Nα-benzoyl-glycine and -alanine.Nα-benzyloxycarbonyl-glycine was hydrolyzed to give equimolar benzyl alcohol and glycine.Equimolar benzoic acid and glycine were produced from Nα-benzoyl-glycine by the enzyme reaction.The Km, k0, and k0/Km values were measured for several substrates.The k0 values varied widely with the amino acid residues.Nα-benzyloxycarbonyl-glycine and Nα-benzoyl-glycine produced relatively small changes in the Km values (0.36 ca. 0.10 mM) and the k0/Km values (99440 ca. 202000 M-1 sec-1).The rate of hydrolysis is significantly affected by electron-supplying substituents on the benzene ring.