ライフサイエンスコーパス: thiolester

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1 preferentially to the UBC13 approximately Ub thiolester.

2 ) of the enzyme-bound alpha,beta-unsaturated thiolester.

3 e case of aliphatic hydroxy esters 11a,b and thiolesters 11e-g from the intermediates 2a-c.

4 0 (GTC)/Ile1000 (ATC), which occurs near the thiolester active site of the molecule.

5 acked antiviral activity, while haloalkanoyl thiolesters and non-halogen-bearing analogues frequently

6 sed on the conversion into diastereoisomeric thiolesters and separation by two fractional crystalliza

7 o suggest that the pi-electrons of the enoyl thiolester are polarized when bound at the active site.

8 tivities of E1 and E2 were determined by the thiolester assays.

9 eptable antiviral potency, thus establishing thiolester benzamides per se as a new anti-HIV chemotype

10 st other molecular targets, thus identifying thiolester benzamides, and PATEs in particular, as novel

11 e have identified Ubc9p surfaces involved in thiolester bond and Smt3p-Smt3p chain formation.

12 The residues involved in thiolester bond formation map to a surface we show is th

13 impairs binding to E1 but not Smt3p impairs thiolester bond formation, suggesting that it is the E1

14 have shown that E6AP can form a high energy thiolester bond with ubiquitin and, in the presence of E

15 the reactivity of the Ubc13 approximately Ub thiolester bond.

16 so be coupled to nonlysine residues by ester/thiolester bonds; however, the molecular basis for these

17 ing through -NH-C(=O)- (amide) or -S-C(=O)- (thiolester) bridges.

18 ding to UBC13, as well as with attack on the thiolester by an acceptor ubiquitin, thereby inhibiting

19 hich is acidified by the polarization of the thiolester carbonyl oxygen through hydrogen bonding to t

20 rse of reduction of dienoyl-coenzyme A (CoA) thiolesters catalyzed by the 2,4-dienoyl-CoA reductase f

21 HsUbc9 forms thiolester conjugates with recombinant SUMO-1, but not w

22 h respect to the wild type HsUbc2b-ubiquitin thiolester, demonstrating that ubiquitin binding contrib

23 o human alpha-lactalbumin, HsUbc2b-ubiquitin thiolester exhibits a K(i) of 54 +/- 18 nm and is compet

24 t convert this E2 to the active E2-ubiquitin thiolester form, can substitute for crude cytosol.

25 SG15 capable of stoichiometric ATP-dependent thiolester formation with its human UbE1L activating enz

26 ntitation by stoichiometric (125)I-ubiquitin thiolester formation.

27 nce the 3'-phosphate group of the coenzyme A thiolester has the potential to form a hydrogen bond wit

28 propane ring formation, which is followed by thiolester hydrolysis, yielding free CMA.

29 m ethanethiolate generated the alpha-hydroxy thiolester in high yield and further transformations led

30 R1 did not promote formation of the RUB-ECR1 thiolester, indicating that AXR1 is the major activity i

31 an activating enzyme (E1) and formation of a thiolester intermediate with a conjugating enzyme (E2) p

32 of L-allo-isoleucine to produce an aminoacyl thiolester intermediate.

33 Pyridinioalkanoyl thiolesters (PATEs) exhibited superior anti-HIV-1 activi

34 emical course of reduction of InhA, an enoyl-thiolester reductase from Mycobacterium tuberculosis, wa

35 and kinetic characterization of an analogous thiolester substrate, 3-(N-glycyl-l-cysteinyl)-propanoyl

36 In addition to the thiolester substrate, the catalytic water, which is adde

37 yl or p-coumaroyl moieties from a coenzyme A-thiolester to malate but not shikimate.

38 yl or p-coumaroyl moieties from a coenzyme A-thiolester to shikimate but not malate, whereas HCT2 tra

39 of the free ubiquitin in cells is present as thiolesters to the components of the conjugation pathway

40 nt reduction of 2,4-dienoyl-coenzyme A (CoA) thiolesters to the resulting trans-3-enoyl-CoA.

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