ライフサイエンスコーパス: L-threonine

1 e substituted with a phosphorylated N-methyl-l-threonine.

2 iably discriminate sucrose from L-serine and L-threonine.

3 ric regulation by the end product amino acid L-threonine.

4 ite-repressing sugars and in the presence of L-threonine.

5 1.3 uM in the presence of millimolar ATP and L-threonine.

6 ly, two residues were found to interact with L-threonine.

7 moc-phospho(1-nitrophenylethyl-2-cyanoethyl)-L-threonine 2, and N-alpha-Fmoc-phospho(1-nitrophenyleth

8 omain-deficient mutant of RGS7, and UBO-QIC {L-threonine,(3R)-N-acetyl-3-hydroxy-L-leucyl-(aR)-a-hydr

9 UF1537 family, and a member of the 4-hydroxy-l-threonine 4-phosphate dehydrogenase (PdxA) oxidative d

10 e with an unusual domain architecture and an L-threonine:4-nitrophenylacetaldehyde transaldolase resp

11 L-Threonine acetaldehyde-lyase (threonine aldolase, TA)

12 lain preferences for L-allo-threonine versus L-threonine among TA family members.

13 subunit (Cy-Cy-A-C-PCP-C) to utilize various L-threonine analogues and found the beta-functionalized

14 fied PduX-His(6) catalyzed the conversion of l-threonine and ATP to L-threonine-O-3-phosphate and ADP

15 Although L-threonine and L-allo-threonine are substrates for T. m

16 Menten kinetics with respect to both ATP and l-threonine and nonlinear regression was used to determi

17 the first enzyme shown to phosphorylate free L-threonine and the first L-threonine kinase shown to fu

18 pha-amino diazoketones from L-isoleucine and L-threonine and to the preparation of a diastereomeric p

19 al structure of CqsA in the presence of PLP, l-threonine, and decanoyl-CoA shows a trapped external a

20 Amino acids such as l-proline, l-threonine, and l-methionine elicited complex current-v

21 zyme (OAS, N-acetyl-L-serine [NAS], O-acetyl-L-threonine, and N-acetyl-L-threonine) were individually

22 ,3-dihydroxybenzoate (DHB), two molecules of L-threonine, and one of norspermidine.

23 rbations of the aminoacyl-tRNA biosynthesis, L-threonine, and renal secretion of organic electrolytes

24 activates and covalently loads its PCP with L-threonine, and together with vibriobactin synthetase p

25 rB2, chlorinates C4 of its native substrate, l-threonine appended to the carrier protein, SyrB1, but

26 Starting with L-threonine as a chiron, a series of stereocontrolled co

27 H, and VibF, using 2,3-dihydroxybenzoate and L-threonine as precursors to two (dihydroxyphenyl)methyl

28 H, and VibF, using 2,3-dihydroxybenzoate and L-threonine as precursors to two 2,3-dihydroxyphenyl- (D

29 se may be attributable to the elimination of L-threonine binding to the effector sites, which activat

30 ing, and Ser-253 and Ser-255 are critical to l-threonine binding whereas Ser-100 is essential to cata

31 ective for para-aminobenzoate, pyridoxine or l-threonine biosynthesis exhibit substantially decreased

32 further study the interactions with ATP and L-threonine, both substrates of TsaC in the biosynthesis

33 protein functions to transport L-serine and L-threonine by sodium transport into the cell.

34 trate that single crystals of the amino acid L-threonine could be used as optical waveguides and filt

35 valuated using solutions containing 0.03-24% L-threonine, D-threonine, L-leucine, L-lysine, L-glutami

36 dcABCDEFG operon, which encodes an anaerobic L-threonine-degradative pathway.

37 ep biochemical pathway involving the enzymes L-threonine dehydrogenase (EC 1.1.1103) and 2-amino-3-ke

38 Subsequently, we used a recombinant T. cruzi L-threonine dehydrogrenase (TcTDH) to screen the Chagas

39 mations are promoted by a readily accessible l-threonine-derived aminophenol-based boryl catalyst, af

40 In the presence of an L-threonine-derived bifunctional phosphine, 3,4-dihydrop

41 ized for the first time by 3-acylation of an L-threonine-derived tetramic acid with enantiopure 2-met

42 imilar to the taste of sucrose, L-serine and L-threonine generate distinctive percepts.

43 The inhibition of LpxC by a novel N-aroyl-l-threonine hydroxamic acid (CHIR-090) from a recent pat

44 CHIR-090, a novel N-aroyl-l-threonine hydroxamic acid, is a potent, slow, tight-bi

45 erved increased accumulation of L-serine and L-threonine in replicative old cells of Saccharomyces ce

46 SyrB2, which chlorinates L-threonine in the syringomycin biosynthetic pathway, be

47 gate the kinetic and catalytic mechanisms of l-threonine kinase from any organism.

48 ide, which was the expected phenotype for an L-threonine kinase mutant.

49 phosphorylate free L-threonine and the first L-threonine kinase shown to function in coenzyme B(12) s

50 studies presented here show that PduX is an L-threonine kinase used for AdoCbl synthesis.

51 The PduX enzyme of Salmonella enterica is an l-threonine kinase used for the de novo synthesis of coe

52 yme of Salmonella enterica is shown to be an L-threonine kinase used for the de novo synthesis of coe

53 e, providing further support that PduX is an L-threonine kinase.

54 ids that includes l-asparagine, l-glutamine, l-threonine, l-arginine, l-glycine, l-proline, l-serine,

55 sphate, an intermediate in the production of L-threonine, L-isoleucine, and in higher plants, L-methi

56 iculty discriminating sucrose from L-serine, L-threonine, maltose, fructose, and glucose.

57 We report that l-threonine may substitute for l-serine in the beta-subs

58 CobD was shown to decarboxylate L-threonine O-3-phosphate to yield (R)-1-amino-2-propano

59 zed the conversion of l-threonine and ATP to L-threonine-O-3-phosphate and ADP.

60 f the pyridoxal 5'-phosphate (PLP)-dependent L-threonine-O-3-phosphate decarboxylase (CobD) from Salm

61 ed from a protein with different function is L-threonine-O-3-phosphate decarboxylase (CobD) from Salm

62 e, CobD is the first enzyme reported to have L-threonine-O-3-phosphate decarboxylase activity, and co

63 equence signature for distinguishing between L-threonine-O-3-phosphate decarboxylase and histidinol p

64 or by supplementation of growth medium with L-threonine-O-3-phosphate, providing further support tha

65 te of CqsA and that another substrate may be l-threonine or l-2-aminobutyric acid.

66 nt (PLP) enzyme that catalyzes conversion of L-threonine or L-allo-threonine to glycine and acetaldeh

67 lexibility in TsaC that may be important for L-threonine recognition, ATP activation, and/or protein/

68 A covalently bound N-acetyl-l-threonine residue demonstrates the geometry of C3b att

69 thesized in 60% yield from L-serine and allo-L-threonine, respectively.

70 solution obtained in the presence of PLP and l-threonine reveals an external aldimine that has lost t

71 r results show that L-allothreonine, but not L-threonine, serves as an effective substrate.

72 steps have occurred, again with loss of the l-threonine side chain.

73 veals an external aldimine that has lost the l-threonine side chain.

74 The conversion of L-threonine to glycine in both prokaryotes and eukaryote

75 lso present preliminary data suggesting that L-threonine transaldolases might be useful for the prepa

76 nd identifies further gene clusters encoding L-threonine transaldolases.

77 forming event during GlyU biosynthesis as an l-threonine:uridine-5'-aldehyde transaldolase.

78 L-Threonine was similarly oxidized to 2-hydroxypropanal

79 ne [NAS], O-acetyl-L-threonine, and N-acetyl-L-threonine) were individually tested for the ability to

80 xtent by phospho-d-serine but not by phospho-l-threonine, which is consistent with the coreceptor fun

81 ta-OH amino acids while avoiding activity on l-threonine, which is needed for ObiH activity.