ライフサイエンスコーパス: homocitrate

1 insertion of molybdenum and coordination by homocitrate.

2 hesis prior to the incorporation of Mo and R-homocitrate.

3 e, 9S, 1Mo, one unidentified light atom, and homocitrate.

4 from its simple constituents, Fe, S, Mo, and homocitrate.

5 binding before AcCoA and CoA released before homocitrate.

6 the L-cluster) prior to insertion of Mo and homocitrate.

7 e centered radical possibly originating from homocitrate.

8 luster accumulating on VnfX does not contain homocitrate.

9 ter prior to the insertion of molybdenum and homocitrate.

10 ster ([Fe(8)S(7)]) and FeMoco ([MoFe(7)S(9)C.homocitrate]).

11 ) and alpha-ketoglutarate (alpha-KG) to give homocitrate and CoA.

12 ion of AcCoA and alpha-ketoglutarate to give homocitrate and CoA.

13 in the hydrolysis of homocitryl-CoA to give homocitrate and CoA.

14 tyl-coenzyme A and 2-oxoglutarate to form 3R-homocitrate and coenzyme A.

15 tive vs AcCoA suggesting binding of CoA to E:homocitrate and E:alpha-ketoglutarate.

16 ain atomic contributions from Mo(4+) and the homocitrate and from the central prismane Fe sites and m

17 num cofactor (FeMo-co) composed of 7Fe-9S-Mo-homocitrate and one not-yet-identified atom, which proba

18 wn that the homologues of cis-homoaconitate, homocitrate, and (-)-threo-isohomocitrate serve as inter

19 omposed of 7 iron, 9 sulfur, 1 molybdenum, 1 homocitrate, and 1 unidentified light atom.

20 -regenerating system, dithionite, molybdate, homocitrate, and at least NifB-co (the metabolic product

21 FeMo-co is composed of 7Fe, 9S, Mo, R-homocitrate, and one unidentified light atom.

22 Here we show that Mo and homocitrate are incorporated into the Fe/S core of the F

23 2 occurs at the FeMo-cofactor, a 7Fe-9S-Mo-C-homocitrate cluster.

24 ontains an [8Fe-7S] cluster and a [7Fe-9S-Mo-homocitrate] cluster, respectively designated the P-clus

25 gnated the M-cluster, this [MoFe(7) S(9) C(R-homocitrate)] cofactor is synthesized via the transforma

26 f the active-site FeMo-cofactor [7Fe-9S-C-Mo-homocitrate] contained within the MoFe protein alpha-sub

27 llic active-site FeMo-cofactor (Fe(7)MoS(9)C-homocitrate) contains a carbide (C(4-)) centered within

28 In the present study, we show the homocitrate-dependent transfer of (49)V label from VnfX

29 tic center of nitrogenase, the [Mo:7Fe:9S:C]:homocitrate FeMo cofactor, is a S=3/2 system with a rhom

30 a Mo/homocitrate insertase that mobilizes Mo/homocitrate for the maturation of FeMoco precursor on Ni

31 group called P-cluster and a [7Fe-9S-C-Mo-R-homocitrate] group called FeMo-co.

32 :9S:1C] metallocluster coordinated with an R-homocitrate (HCA) molecule.

33 ith acetylCoA to form, respectively, the (R)-homocitrate homologues of (R)-2-hydroxy-1,2,5-pentanetri

34 enase contains molybdenum, iron, sulfur, and homocitrate in a ratio of 1:7:9:1.

35 site metal cluster (FeMo-co, Fe(7)S(9)CMo-R-homocitrate) in Mo-dependent nitrogenase requires the pr

36 The homocitrate incorporation reaction and the insertion of

37 we show that the Fe protein can act as a Mo/homocitrate insertase that mobilizes Mo/homocitrate for

38 level of nifV expression is induced excrete homocitrate into the growth medium.

39 gest that there is in vitro incorporation of homocitrate into the V-Fe-S cluster associated with VnfX

40 ore prior to the insertion of molybdenum and homocitrate into this core.

41 binds and reduces N2 at the [Fe7, Mo, S9, X, homocitrate] iron-molybdenum cofactor (FeMo-co).

42 The DFT calculations indicate that the homocitrate ligand of the cofactor can become monodentat

43 -O7 (hydroxyl) distance that switches the Mo-homocitrate ligation from bidentate to monodentate.

44 rate reduction is provided by a [7Fe-9S-Mo-X-homocitrate] metallocluster, where X is proposed to be a

45 We also establish that only molybdate, homocitrate, MgATP, and Fe protein are essential for FeM

46 ynthesis system, NifH, NifNE, NifB-cofactor, homocitrate, MgATP, and reductant, are present.

47 Further, we establish that Mo/homocitrate mobilization by the Fe protein likely involv

48 ion of N(2) to NH(3) at its cofactor, an [(R-homocitrate)MoFe(7)S(9)C] cluster synthesized via the fo

49 l homolog of the M-cluster (or cofactor; [(R-homocitrate)MoFe(7)S(9)C]) of NifDK.

50 on cluster as its active-site co-factor ([(R-homocitrate)MoFe(7)S(9)C], FeMoco)(1,2), and the sulfur-

51 ework of the FeMo-cofactor; depletion of the homocitrate moiety; diminished density around the S2B be

52 r atoms, an interstitial light atom, and one homocitrate molecule.

53 hen incubated with the necessary substrates (homocitrate, molybdate, and S-adenosylmethionine [SAM]),

54 Structural analogues of homocitrate prevent the acetylene reduction ability of t

55 ns, together with Fe(2+), S(2-), MoO4(2-), R-homocitrate, S-adenosyl methionine, and Mg-ATP, is suffi

56 and dehydrated to cis-homoaconitate with (S)-homocitrate serving as an intermediate.

57 One type is a 7Fe-9S-Mo-C-homocitrate species designated FeMo-cofactor, which prov

58 e protein corresponds to a [MoFe(7)S(9)C-(R)-homocitrate] species designated FeMo-cofactor, whose bio

59 Homocitrate synthase (acetyl-coenzyme A: 2-ketoglutarate

60 Homocitrate synthase (acetyl-coenzyme A:2-ketoglutarate

61 Homocitrate synthase (HCS) catalyzes one of the regulate

62 Homocitrate synthase (HCS) catalyzes the first and commi

63 The enzyme homocitrate synthase (HCS) catalyzes the first step in l

64 Homocitrate synthase (HCS) catalyzes the first step of l

65 d kinetic mechanism for the histidine-tagged homocitrate synthase (HCS) from Saccharomyces cerevisiae

66 st enzyme in the alpha-aminoadipate pathway, homocitrate synthase (HCS), is the target of the feedbac

67 Lys20 was initially described as homocitrate synthase (HCS), the first enzyme in the lysi

68 The homocitrate synthase from Thermus thermophilus (TtHCS) i

69 us is unexpected given previous reports that homocitrate synthase is present in mitochondria and the

70 open reading frames are predicted to encode homocitrate synthase isozymes of 47 and 49 kDa, respecti

71 The localization of homocitrate synthase to the nucleus is unexpected given

72 For example, the lysine biosynthetic enzyme homocitrate synthase was recently shown to have unexpect

73 Homocitrate synthase was used as an example in terms of

74 t predict the regulatory kinetic behavior of homocitrate synthase were derived, and simulation of the

75 kinetic isotope effect of 1 is measured for homocitrate synthase, while a small pH-independent prima

76 ain information on the chemical mechanism of homocitrate synthase.

77 tallocluster called FeMo-cofactor [7Fe-9S-Mo-homocitrate] that exhibits an S = 3/2 EPR signal in the

78 hown to catalyze both the dehydration of (R)-homocitrate to form cis-homoaconitate, and its hydration

79 te rather than the complete isomerization of homocitrate to homoisocitrate.

80 FeMo-co from Fe(2+), S(2-), MoO4(2-), and R-homocitrate using only purified Nif proteins.

81 n-molybdenum cofactor (FeMoco) ([Mo-7Fe-9S-X-homocitrate]), whereas the other contains a presumed P c

82 MoFe protein, the FeMo-cofactor ([7Fe-9S-Mo-homocitrate-X]; FeMo-co) only after the MoFe protein has