ライフサイエンスコーパス: sulfinic acid

1 ate Cys levels through converting Cys to Cys sulfinic acid.

2 enation of cysteine by O(2) to give cysteine sulfinic acid.

3 yzes the oxidation of l-cysteine to cysteine sulfinic acid.

4 on and protect against hyperoxidation to the sulfinic acid.

5 the thiol residue of the cysteine switch to sulfinic acid.

6 cysteine switch domain had been converted to sulfinic acid.

7 e substituted sulfinamides that hydrolyze to sulfinic acids.

8 tions based on the unique nucleophilicity of sulfinic acids.

9 cts; other minor products including cysteine sulfinic acid (+32 Da mass shift) and serine (-16 Da mas

10 is subsequently hydrolyzed back to cysteine sulfinic acid and AMP in a futile cycle.

11 a comeback: The inefficient condensation of sulfinic acid and aryl nitroso compounds has been transf

12 cs of two alternative substrates: L-cysteine sulfinic acid and d-aspartate.

13 competitive C-S bond cleavage giving phenyl sulfinic acid and ionization to diphenyl sulfide radical

14 , C-S bond cleavage, finally leading to aryl sulfinic acid and sensitized oxidation leading to S-oxid

15 oxy nitroso compounds to AhpC C165S yields a sulfinic acid and sulfinamide modification.

16 Here we demonstrate that sulfinic acids and nitrosothiols react to form a stable

17 alyze decarboxylation of aspartate, cysteine sulfinic acid, and cysteic acid to beta-alanine, hypotau

18 enic acid oxoform from the thiol, disulfide, sulfinic acid, and S-nitrosated forms of cysteine while

19 In addition, the MS data identified sulfinic acid as the irreversibly inactivated enzyme spe

20 dize further to the irreversibly inactivated sulfinic acid, as determined by using kinetic partitioni

21 herited parkinsonism, readily forms cysteine-sulfinic acid at a conserved cysteine residue (Cys106 in

22 We observed a cysteine-sulfinic acid at C106 in crystalline DJ-1 but no modific

23 e that PCO dioxygenase activity produces Cys-sulfinic acid at the N terminus of an ERF-VII peptide, w

24 L-cysteine sulfinic acid bound with higher affinity than L-aspartat

25 the conversion of cysteine (Cys) to cysteine sulfinic acid by an unclarified mechanism.

26 ne begins with its sulfoxidation to cysteine sulfinic acid by the enzyme cysteine dioxygenase (CDO).

27 ulfinated proteins, confirming that a single sulfinic acid can react with a nitrosothiol to form a th

28 Prior work showed that L-cysteine sulfinic acid competitively inhibits this enzyme by inte

29 that results in the accumulation of cysteine sulfinic acid (CSA) in glioblastoma.

30 such as homocysteic acid (HCA) and cysteine sulfinic acid (CSA), which may cause seizures and excito

31 oxins (Prxs) undergo reversible oxidation to sulfinic acid (Cys-SO2H) and the reduction reaction is c

32 rx enzymes undergoes reversible oxidation to sulfinic acid (Cys-SO2H) during catalysis, and sulfiredo

33 Among many proteins with cysteine sulfinic acid (Cys-SO2H) residues, the sulfinic forms of

34 duced Cys(34), whereas the levels of Cys(34) sulfinic acid (Cys-SO2H), Cys(34)-sulfonic acid (Cys-SO3

35 s-SOH moiety can react with H2O2 to form Cys sulfinic acid (Cys-SO2H), resulting in inactivation.

36 reaction, the reduction of protein cysteine sulfinic acid, Cys-SO(2)(-).

37 onally relevant reversible and irreversible (sulfinic acid; Cys to dehydroalanine) oxidations of GAPD

38 esizing enzyme in the brain, namely cysteine sulfinic acid decarboxylase (CSAD), is activated when ph

39 enosylhomocysteine (SAH) hydrolase, cysteine sulfinic acid decarboxylase, and oxidation-reduction pat

40 ase B, sarcosine dehydrogenase, and cysteine sulfinic acid decarboxylase, are involved in carbohydrat

41 n enzyme that catalyzes the reduction of Cys-sulfinic acid derivatives of 2-Cys peroxiredoxins (2-Cys

42 d lays the groundwork for the development of sulfinic acid detection methods in biological systems.

43 While cysteine sulfinic acid did not itself constitute a clinically use

44 In physiological buffers, sulfinic acids do not react with iodoacetamide or disulf

45 ine in typical 2-Cys peroxiredoxins (Prx) to sulfinic acid during oxidative stress plays an important

46 sidue can be permanently overoxidized to the sulfinic acid form, and (ii) Sec protects the body of th

47 ntioxidant enzyme peroxiredoxin (Prx) to the sulfinic acid form, Prx-SO(2)(-).

48 rovides molecular evidence of N-terminal Cys-sulfinic acid formation and arginylation by N-end rule p

49 Several stimuli, including peroxide-mediated sulfinic acid formation at the active site cysteine, hav

50 homologues are likely stabilized by cysteine-sulfinic acid formation but destabilized by further oxid

51 For proteins such as Prx VI and GAPDH, sulfinic acid formation might be an irreversible process

52 eroxiredoxin, whose oxidative stress-induced sulfinic acid formation turns the peroxidase into a mole

53 The oxidation of Cys106 to the sulfinic acid had minimal effect on the structural prope

54 The formation of cysteine-sulfinic acid has recently become appreciated as a modif

55 and generation of cysteine sulfonic acid and sulfinic acid; however, the rate of oxidation is signifi

56 in DJ-1 is oxidized readily to the cysteine-sulfinic acid in both flies and humans, and this may reg

57 " is oxidized to either cysteine sulfenic or sulfinic acid in the two molecules in the asymmetric uni

58 Unlike either the cysteine sulfinic acid interaction with AS-B or the sulfoximine i

59 presumably via the unstable doubly oxidized sulfinic acid intermediate.

60 into a chemoselective process that converts sulfinic acid into stable cyclic sulfonamide analogues (

61 therefore conclude that formation of Cys106-sulfinic acid is a key modification that regulates the p

62 Here, we demonstrate that cysteine sulfinic acid is also a partial substrate for E. coli as

63 on of two cysteine thiolates to sulfenic and sulfinic acids is essential for enzyme activity.

64 olism, the oxidation of cysteine to cysteine sulfinic acid, is catalyzed by cysteine dioxygenase (CDO

65 increased oxidant stress confirmed cysteinyl sulfinic acid (m/z 435), sulfonic acid (m/z 443), and di

66 Conversely, substitution with the sulfinic acid mimic aspartic acid resulted in constituti

67 e, the scope and biological role of sulfenic/sulfinic acid modifications have been recently expanded

68 The Cys(52) sulfinic acid moiety was substituted by mutating this re

69 The reduction of the cysteine sulfinic acid moiety within the active site of the Prx b

70 direct quantitative determination of methane sulfinic acid (MSA) produced by hydroxyl radical oxidati

71 the addition of two oxygen atoms to form the sulfinic acid of Cys106 (2O DJ-1) (no 1O oxidized state

72 as well as cysteine oxidation determined as sulfinic acid on alpha-Cys-104 and sulfonic acid on alph

73 by intraseptal injection of L-AP4, cysteine sulfinic acid or DHPG.

74 site disulfide and a reduction irreversible sulfinic acid or sulfinamide modification at Cys244.

75 The latter was converted to closo-1,12-bis(sulfinic acid)-p-carborane (13) via H(+)-exchange.

76 obtained directly in 88% yield by heating 1-sulfinic acid-p-carborane (17) in H(2)O(2) (30%).

77 to the sulfinic moiety of PrxI to generate a sulfinic acid phosphoryl ester (Prx-Cys-S(=O)OPO3(2-)).

78 n (18)O exchange study revealed that the Prx sulfinic acid phosphoryl ester is rapidly formed and hyd

79 ormation between simple terminal alkynes and sulfinic acids provides access to various alpha-substitu

80 resh muscle or kidney extracts with cysteine sulfinic acid resulted in the detection of hypotaurine o

81 In addition, although sulfinic acid [RS(O)OH] formation is observed upon prolo

82 One-pot reactions of sulfinic acid salts (produced from organometallic reagen

83 The sulfinic acid salts were prepared from the reaction of t

84 various other proteins are also oxidized to sulfinic acid, suggesting that formation of Cys-SO2H mig

85 rometric analysis identified the products as sulfinic acid, sulfonic acid, and a dimer containing a d

86 function of Srx is the reduction of cysteine sulfinic acid to sulfenic acid in proteins subject to ox

87 E18Q, allow Cys106 to be oxidized to Cys106-sulfinic acid under mild conditions.

88 cells, the initial formation rate of methane sulfinic acid was significantly lower in cells containin

89 ese proteins to oxidize cysteine to cysteine sulfinic acid was then compared against recombinant rat

90 duct analysis indicated cystine and cysteine sulfinic acid were the major photooxidation products.

91 alyzes the oxidation of cysteine to cysteine sulfinic acid, which is the first major step in cysteine

92 roduct from nucleophilic addition eliminates sulfinic acid, yielding a propargylic diazene that perfo