943-80-6Relevant articles and documents
Deracemization and stereoinversion to aromatic d-amino acid derivatives with ancestral l-amino acid oxidase
Nakano, Shogo,Minamino, Yuki,Hasebe, Fumihito,Ito, Sohei
, p. 10152 - 10158 (2019/10/19)
Enantiomerically pure amino acid derivatives could be foundational compounds for peptide drugs. Deracemization of racemates to l-amino acid derivatives can be achieved through the reaction of evolved d-amino acid oxidase and chemical reductants, whereas deracemization to d-amino acid derivatives has not progressed due to the difficulty associated with the heterologous expression of l-amino acid oxidase (LAAO). In this study, we succeeded in developing an ancestral LAAO (AncLAAO) bearing broad substrate selectivity (13 l-amino acids) and high productivity through an Escherichia coli expression system (50.7 mg/L). AncLAAO can be applied to perform deracemization to d-amino acids in a similar way to deracemization to l-amino acids. In fact, full conversion (>99% ee, d-form) could be achieved for 16 racemates, including nine d,l-Phe derivatives, six d,l-Trp derivatives, and a d,l-phenylglycine. Taken together, we believe that AncLAAO could be a key enzyme to obtain optically pure d-amino acid derivatives in the future.
Identification of new peptide amides as selective cathepsin L inhibitors: The first step towards selective irreversible inhibitors?
Torkar, Ana,Lenar?i?, Brigita,Lah, Tamara,Dive, Vincent,Devel, Laurent
supporting information, p. 2968 - 2973 (2013/06/27)
A small library of peptide amides was designed to profile the cathepsin L active site. Within the cathepsin family of cysteine proteases, the first round of selection was on cathepsin L and cathepsin B, and then selected hits were further evaluated for binding to cathepsin K and cathepsin S. Five highly selective sequences with submicromolar affinities towards cathepsin L were identified. An acyloxymethyl ketone warhead was then attached to these sequences. Although these original irreversible inhibitors inactivate cathepsin L, it appears that the nature of the warhead drastically impact the selectivity profile of the resulting covalent inhibitors.
Photoswitching of the Enzymatic Activity of Semisynthetic Ribonuclease S' Bearing Phenylazophenylalanine at a Specific Site
Hamachi, Itaru,Hiraoki, Takashi,Yamada, Yasuhiro,Shinkai, Seiji
, p. 704 - 706 (2007/10/03)
Photoswitching of the enzymatic activity of ribonuclease S' was successfully carried out by site specific incorporation of phenylazophenylalanine into S-peptide skeleton by semisynthesis.