2598-46-1Relevant academic research and scientific papers
Rationally engineered variants of S-adenosylmethionine (SAM) synthase: Reduced product inhibition and synthesis of artificial cofactor homologues
Dippe,Brandt,Rost,Porzel,Schmidt,Wessjohann
supporting information, p. 3637 - 3640 (2015/03/30)
S-Adenosylmethionine (SAM) synthase was engineered for biocatalytic production of SAM and long-chain analogues by rational re-design. Substitution of two conserved isoleucine residues extended the substrate spectrum of the enzyme to artificial S-alkylhomocysteines. The variants proved to be beneficial in preparative synthesis of SAM (and analogues) due to a much reduced product inhibition. This journal is
Palatability of aquaculture feed
-
, (2008/06/13)
A method for enhancing the palatability of aquaculture food, the method comprising treating the food with a compound of Formula I: wherein R1, R2, R3, and n are as defined herein, are disclosed.
Deamination and γ-Addition Reactions of Vinylglycine Catalyzed by Yeast Kynurenine Aminotransferase, and Suicidal Inactivation of the Enzyme during Its Processing
Asada, Yasuhiko,Tanizawa, Katsuyuki,Yonaha, Kazuo,Soda, Kenji
, p. 2873 - 2878 (2007/10/02)
Kynurenine aminotransferase from a yeast, Hansenula schneggii, has been found to catalyze the deamination of an olefinic amino acid, L-vinylglycine, to form α-ketobutyrate and ammonia.The maximum rate of deamination was 0.17 μmol/mg/min at 25 deg C (pH 8.0), which is approximately 1percent of the rate of transamination between L-kynurenine and α-ketoglutarate.Concomitantly with the catalysis, the enzyme lost both the deaminase and aminotransferase activities in a time-dependent manner.The inactivation was irreversible and followed pseudo-first-order kinetics at various concentrations of L-vinylglycine.The Michaelis constant for L-vinylglycine in the inactivation reaction was essentially the same as that in the deamination.These results indicate that the two reactions proceed through a common intermediary complex, and L-vinylglycine acts as a suicide inactivator for the enzyme.The apoenzyme neither catalyzed the deamination nor was inactivated by L-vinylglycine.The enzyme also catalyzes the γ-addition reaction of L-vinylglycine in the presence of alkanethiols producing the corresponding S-substituted homocysteines.
A SIMPLE PREPARATION OF S-ALKYL HOMOCYSTEINE DERIVATIVES: S-PHOSPHONOMETHYL HOMOCYSTEINES AS INHIBITORS OF GLUTAMINE SYNTHETASE
Logusch, Eugene W.
, p. 6055 - 6058 (2007/10/02)
A facile synthesis of S-alkyl homocysteines is described which features the coupling of sodium alkyl thiolates with methyl 4-bromo-2-phthalimidobutyrate, followed by hydrolysis.This approach is exemplified by the synthesis of S-phosphonomethyl homocysteine sulfone, a new inhibitor of the enzyme glutamine synthetase.
