ライフサイエンスコーパス: alanine racemase

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 arrier crossing for proton-transfer steps in alanine racemase.

5 predicted for all of the ionizable groups in alanine racemase.

6 by a hydrogen bond network such as found 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

10 The D-alanine racemase activities of wild-type and recombinant

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

13 ntibiotic that inhibits d-alanine ligase and alanine racemase activity.

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

16 e alanine racemization reaction catalyzed by alanine racemase (AlaR).

17 e site pocket, in the context of other known alanine racemases, allows us to propose the inclusion of

18 The putative biosynthetic alanine racemase Alr showed broad substrate specificity,

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

21 t proteins, one of which is a spore-specific alanine racemase (Alr).

22 (2-AA)/PLP adduct forms on the biosynthetic alanine racemase, Alr, indicating the presence of 2-amin

23 ned the glutamate decarboxylase (gadA) and D-alanine racemase (alrA) genes was identified.

24 Gram-negative and -positive bacteria, making alanine racemase an attractive target for antibacterials

25 Cycloserine acts as a suicide inhibitor of alanine racemase and as such, serves as an antimicrobial

26 ell wall peptidoglycan biosynthesis enzymes: alanine racemase and D-alanine:D-alanine ligase.

27 ures of the Michaelis complex formed between alanine racemase and its amino acid substrate.

28 for catalysis of transamination, while both alanine racemase and O-acetylserine sulfhydrylase are ex

29 The other two proteins identified were alanine racemase and superoxide dismutase, both of which

30 similar to that of Bacillus and Pseudomonas alanine racemases and includes both an alpha/beta-barrel

31 encoding homologs of alanine dehydrogenase, alanine racemase, and alanine permease.

32 Alanine racemases are ubiquitous prokaryotic enzymes pro

33 structure of the complex between L-Ala-P and alanine racemase at 1.6 A resolution.

34 L-Ala-P is an effective inhibitor of alanine racemase because, upon formation of the external

35 milar to that of Bacillus stearothermophilus alanine racemase, but the rotation between domains diffe

36 dimine derivative and potent inactivation of alanine racemase by this compound.

37 One of the enzymes is Alr, an alanine racemase capable of converting the spore germina

38 The pyridoxal phosphate dependent alanine racemase catalyzes the interconversion of L- and

39 Alanine racemase catalyzes the pyridoxal phosphate-depen

40 In contrast, analysis of alanine racemase clearly refutes claims that global anal

41 As a proof of concept, we applied the D-alanine racemase complementation system to our Listeria

42 Conversely, the putative catabolic alanine racemase DadX showed narrow substrate specificit

43 The structure of the catabolic alanine racemase, DadX, from the pathogenic bacterium Ps

44 mid that is retained by complementation of D-alanine racemase-deficient mutant strains both in vitro

45 Alanine racemase (EC 5.1.1.1) catalyzes the interconvers

46 bacterial cell walls is fulfilled in part by alanine racemase (EC 5.1.1.1), a pyridoxal 5'-phosphate

47 he interconversion of L- and D-alanine-d3 by alanine racemase from Bacillus stearothermophilus direct

48 Free energy profiles for alanine racemase from Bacillus stearothermophilus have b

49 The molecular structure of alanine racemase from Bacillus stearothermophilus was de

50 The structure of alanine racemase from Bacillus stearothermophilus with t

51 n of pyridoxal phosphate in the structure of alanine racemase from Bacillus stearothermophilus.

52 based on the alignment of VanT with the Air alanine racemase from Bacillus stearothermophilus.

53 ing the pyridoxal phosphate-dependent enzyme alanine racemase from Geobacillus stearothermophilus are

54 We report the crystal structure of alanine racemase from Mycobacterium tuberculosis (Alr(Mt

55 alpha-isomer, the catalysis of a promiscuous alanine racemase from Pseudomonas putida (KT2440) was co

56 Alanine racemase further lowers the alpha-proton acidity

57 t control the synthesis of this compound, an alanine racemase gene (dal) and a D-amino acid aminotran

58 fferences among pseudomonads with respect to alanine racemase genes that may point to different roles

59 However, alanine racemase has a positively charged arginine held

60 nds to about one-half of the burden borne by alanine racemase in catalysis of deprotonation of alanin

61 of the inhibitor, we propose a mechanism of alanine racemase inactivation by cycloserine.

62 by d-[1-(13)C]alanine (in the presence of an alanine racemase inhibitor) reveal three different carbo

63 D-[1-(13)C]alanine, [(15)N]glycine, and the alanine racemase inhibitor, alaphosphin.

64 th D-alanine production, was prevented by an alanine racemase inhibitor, and required L-alanine.

65 Many endospore-forming bacteria embed alanine racemases into their spore coats, and these enzy

66 chemical means by which cycloserine inhibits alanine racemase is unknown.

67 n in-frame deletion mutation in the gene for alanine racemase lost only the ability to grow on D-alan

68 The alanine racemase monomer is composed of two domains, an

69 -isomer case) of Bacillus stearothermophilus alanine racemase on cycloserine inactivation.

70 amination, but not to reactions catalyzed by alanine racemase or O-acetylserine sulfhydrylase.

71 er, these spores retained half the amount of alanine racemase presumed to be associated with the exos

72 ervations indicate that cycloserine inhibits alanine racemase production of D-Ala in E. coli and demo

73 ipopolysaccharide O antigen ligase), or alr (alanine racemase) resulted in increased urothelial inter

74 for catalysis of amino-acid racemization by alanine racemase shows that the enzyme causes a ca 2 x 1

75 Also, as observed in other alanine racemase structures, PLP adopts a conformation t

76 Cycloserine is a known alanine racemase suicide substrate, although its mechani

77 ator of all purified Gram-positive bacterial alanine racemases that have been tested.

78 In comparison to structurally related alanine racemase, the two domains are rotated 27 degrees

79 ild-type and gerP spores with or without all alanine racemases were almost identical.

80 The presence of alanine dehydrogenase and alanine racemase, which are uniquely present among the A

81 al structures of Bacillus stearothermophilus alanine racemase, which corroborates the spectroscopy vi

82 s unstable exosporium also lacked the enzyme alanine racemase, which is normally tightly associated w

83 It is concluded that TOXG encodes an alanine racemase whose function is to synthesize D-Ala f

84 oretical model for the complex of the enzyme alanine racemase with its natural substrate (L-alanine)