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1 kinetic and equilibrium isotope effects for alanine racemase.
2 , E. coli CBL (fold type I) is a promiscuous alanine racemase.
3 kinetic isotope effect (KIE) methodology to alanine racemase.
4 predicted for all of the ionizable groups in alanine racemase.
5 by a hydrogen bond network such as found in alanine racemase.
6 arrier crossing for proton-transfer steps in alanine racemase.
7 D-amino acid dehydrogenase and the catabolic alanine racemase.
8 nt site in the C-terminal domain, typical of alanine racemases.
9 nd begins 7 bp downstream of dadX (catabolic alanine racemase; 26.55 min) and ends at a position in t
11 4%) inhibited by D-cycloserine, whereas host alanine racemase activity was almost totally inhibited (
12 r centrifugation of sonicated cells, whereas alanine racemase activity was located almost exclusively
14 t formed between d-cycloserine and d-a-AT or alanine racemase (Ala-Rac) in that the thiophene ring of
15 hate (PLP) linked as an internal aldimine in alanine racemase (AlaR), aspartate aminotransferase (Asp
17 e site pocket, in the context of other known alanine racemases, allows us to propose the inclusion of
19 cripts of glutamine synthetase I (glnA1) and alanine racemase (alr) modestly increased the inhibitory
20 ative of fold type III, the Escherichia coli alanine racemase (ALR), is a promiscuous cystathionine b
22 (2-AA)/PLP adduct forms on the biosynthetic alanine racemase, Alr, indicating the presence of 2-amin
23 ine analog d-cycloserine (DCS), which blocks alanine racemase (Alr1) and d-alanine ligase (Ddl) and i
26 Gram-negative and -positive bacteria, making alanine racemase an attractive target for antibacterials
27 Cycloserine acts as a suicide inhibitor of alanine racemase and as such, serves as an antimicrobial
28 an alanine analogue antibiotic that inhibits alanine racemase and d-alanine ligase required for d-ala
31 for catalysis of transamination, while both alanine racemase and O-acetylserine sulfhydrylase are ex
33 similar to that of Bacillus and Pseudomonas alanine racemases and includes both an alpha/beta-barrel
35 (ODC, ADC, LDC), respectively, from both the alanine racemase (AR) and aspartate aminotransferase (AA
39 milar to that of Bacillus stearothermophilus alanine racemase, but the rotation between domains diffe
48 mid that is retained by complementation of D-alanine racemase-deficient mutant strains both in vitro
50 bacterial cell walls is fulfilled in part by alanine racemase (EC 5.1.1.1), a pyridoxal 5'-phosphate
52 he interconversion of L- and D-alanine-d3 by alanine racemase from Bacillus stearothermophilus direct
58 ing the pyridoxal phosphate-dependent enzyme alanine racemase from Geobacillus stearothermophilus are
60 alpha-isomer, the catalysis of a promiscuous alanine racemase from Pseudomonas putida (KT2440) was co
62 t control the synthesis of this compound, an alanine racemase gene (dal) and a D-amino acid aminotran
63 fferences among pseudomonads with respect to alanine racemase genes that may point to different roles
65 nds to about one-half of the burden borne by alanine racemase in catalysis of deprotonation of alanin
67 by d-[1-(13)C]alanine (in the presence of an alanine racemase inhibitor) reveal three different carbo
72 n in-frame deletion mutation in the gene for alanine racemase lost only the ability to grow on D-alan
76 er, these spores retained half the amount of alanine racemase presumed to be associated with the exos
77 ervations indicate that cycloserine inhibits alanine racemase production of D-Ala in E. coli and demo
78 ipopolysaccharide O antigen ligase), or alr (alanine racemase) resulted in increased urothelial inter
79 for catalysis of amino-acid racemization by alanine racemase shows that the enzyme causes a ca 2 x 1
85 The presence of alanine dehydrogenase and alanine racemase, which are uniquely present among the A
86 al structures of Bacillus stearothermophilus alanine racemase, which corroborates the spectroscopy vi
87 s unstable exosporium also lacked the enzyme alanine racemase, which is normally tightly associated w
89 oretical model for the complex of the enzyme alanine racemase with its natural substrate (L-alanine)