Abstract:
The present application relates to a mutated Amycoiatopsis sp . TS-1-60 NAAAR that shows improved activity of the enzyme compared with the wild type Amycoiatopsis sp . TS-1-60 NAAAR. The mutated NAAAR is almost five times more active than its wiid type counterpart. The present application also relates to the use of mutated Amycoiatopsis sp . TS-1 -60 NAAAR in the production of enantiomerically pure amino acid from its N-acyl derivative via dynamic kinetic resolution method.
Abstract translation:公开了编码来自属于短杆菌属的微生物的新型NADH氧化酶并具有优异的pH稳定性和热稳定性的DNA。 具体公开的是编码来自属于短杆菌属的微生物的NADH氧化酶的DNA,其选自下列NADH氧化酶(a)和(b):(a)包含SEQ ID NO:18所示的氨基酸序列的NADH氧化酶 ; 和(b)NADH氧化酶,其包含在SEQ ID NO:18所示的氨基酸序列中具有缺失,取代或添加一个或几个氨基酸残基并具有NADH氧化酶活性的氨基酸序列。
Abstract:
The present invention provides a method for producing an L-amino acid using a bacterium of the Enterobacteriaceae family, particularly a bacterium belonging to genus Escherichia or Pantoea , which has been modified to attenuate expression of the yncD gene.
Abstract:
The present invention provides a method for producing an L-amino acid using a bacterium of the Enterobacteriaceae family, particularly a bacterium belonging to genus Escherichia or Pantoea , which has been modified to attenuate expression of the tolC gene.
Abstract:
A method for producing an L-amino acid is described, for example L-threonine, L-lysine, L-histidine, L-phenylalanine, L-arginine, L-tryptophan, or L-glutamic acid, using a bacterium of the Enterobacteriaceae family, wherein the bacterium has been modified to enhance an activity of a wild-type alcohol dehydrogenase encoded by the adhE gene or a mutant alcohol dehydrogenase which is resistant to aerobic inactivation.
Abstract:
There is disclosed a method for producing L-amino acid, for example L-threonine, L-lysine, L-histidine, L-phenylalanine, L-arginine or L-glutamic acid, using a bacterium of the Enterobacteriaceae family, wherein the bacterium has been modified to enhance an activity of D-xylose permease.
Abstract:
A process for the production of optically active (S)- or (R) -ß-amino acids represented by the general formula (II): (II) [wherein R is optionally substituted, alkyl, alkenyl, alkynyl, cycloalkyl, aralkyl, aryl, or heteroaryl; and * represents an asymmetric carbon atom] and optically active (R)- or (S)-ß-amino acid esters represented by the general formula (III): (III) [wherein R and * are each as defined above; and R
Abstract:
A process for production of cyclopropyl-fused pyrrolidine-based inhibitors of dipeptidyl peptidase IV is provided which employs a BOC-protected amine of the structure (3) prepared by subjecting an acid of the structure (1) to reduce amination by treating the acid with ammonium formate, nicotinamide adenine dinucleotide, dithiothreitol and partially purified phenylalanine dehydrogenase/formate dehydrogenase enzyme concentrate (PDH/FDH) and without isolating treating the resulting amine of the structure (2) with di-tert-butyl dicarbonate to form the BOC-protected amine.
Abstract:
The present invention provides a Rhodotorula phenylalanine lyase polypeptide, polynucleotides that encode the polypeptide, and methods of obtaining and using these products. In particular the polypeptide can be employed for the production of phenylalanine, phenylalanine analogs, and optionally active unnatural amino acids having phenylalanine-like structures.
Abstract:
Disclosed are DNA sequences encoding deletion, substitution and/or addition analogs of the E. coli enzyme, chorismate mutase/prephenate dehydratase (CMPD). Preferred expression products include [des-Gln307, des-Ala308, des-Gly309, des-Ala310]CMPD; [Leu306]CMPD; [des-Thr?304, Lys305¿, des-Gln306]CMPD; and [Cys309]CMPD display enzymatic activity of the wild type enzyme but are more resistant to inhibition in the presence of phenylalanine.