ライフサイエンスコーパス: DMAPP

1 DMAPP levels in Bacillus subtilis and Saccharomyces cere

2 DMAPP levels of 23 +/- 4 nmol (g fresh weight)(-1) [ca.

3 DMAPP-tRNA transferase bound tRNA(Phe) with a dissociati

4 in an ordered sequence, with tRNA first and DMAPP second, and the RNA modification reaction occurs i

5 medium with the alcohol analogues of IPP and DMAPP (3-methyl-3-buten-1-ol and 3-methyl-2-buten-1-ol)

6 reactive toward proton addition than IPP and DMAPP but have similar reactivities toward hydrogen atom

7 eria, catalyzes the isomerization of IPP and DMAPP by a protonation-deprotonation mechanism.

8 iate in the pathway, is converted to IPP and DMAPP by the consecutive action of the IspD-H proteins.

9 responsible for converting HMBPP to IPP and DMAPP in the ultimate step in the nonmevalonate pathway.

10 alone, indicating that the ratio of IPP and DMAPP produced via the DOXP pathway is influenced by Lyt

11 llular substrate in Synechocystis to IPP and DMAPP, overcoming flux limitations of the native MEP pat

12 are approximately 50-fold less than IPP and DMAPP, respectively.

13 s from the respective C5-precursors, IPP and DMAPP, whereas one isoprene unit in the ring E of 1 show

14 he enzyme-catalyzed isomerization of IPP and DMAPP.

15 r to those for chain elongation with IPP and DMAPP.

16 (with IPP) were similar to those for IPP and DMAPP; however, values of k(cat) for both analogues were

17 Thus, when ISPP and DMAPP were incubated with FPPase, GSPP accumulated and w

18 Michaelis constants for tRNA(Phe) and DMAPP are 96 +/- 11 nM and 3.2 +/- 0.5 microM, respectiv

19 ynthase were determined for L-tryptophan and DMAPP at 34 and 76 muM, respectively.

20 ulated from kinetic data of L-tryptophan and DMAPP.

21 ze the isomerization of [(14)C]IPP to [(14)C]DMAPP.

22 ficult to study the relationship of cellular DMAPP levels to emission of these volatiles because of t

23 The midday concentration of chloroplastic DMAPP in cottonwood leaves is estimated to be 0.13 to 3.

24 Active recombinant E. coli DMAPP-tRNA transferase is monomeric.

25 In contrast, DMAPP did not bind to the enzyme in the absence of tRNA.

26 ed with deuterium at the (E)-methyl group (d-DMAPP) and a 34% yield of IPP labeled with 1 mol of deut

27 ial product of the IDI-catalyzed reaction (d-DMAPP) is slower than its conversion to d-IPP.

28 uction also exhibit elevated light-dependent DMAPP production, ranging from 110% to 1,063%.

29 l diphosphate:tRNA dimethylallyltransferase (DMAPP-tRNA transferase) catalyzes alkylation of the exoc

30 l diphosphate:tRNA dimethylallyltransferase (DMAPP-tRNA transferase) catalyzes the alkylation of the

31 l diphosphate:tRNA dimethylallyltransferase (DMAPP-tRNA transferase) catalyzes the first step in the

32 hosphate (IPP) to dimethylallyl diphosphate (DMAPP) and then to geranyl diphosphate (GPP).

33 hosphate (IPP) to dimethylallyl diphosphate (DMAPP) in the mevalonate entry into the isoprenoid biosy

34 he substrates for dimethylallyl diphosphate (DMAPP) IPT activity.

35 diphosphate (IPP):dimethylallyl diphosphate (DMAPP) isomerase (IDI-2) is a flavoenzyme that requires

36 en incubated with dimethylallyl diphosphate (DMAPP) or geranyl diphosphate (GPP) to give the correspo

37 osphate (IPP) and dimethylallyl diphosphate (DMAPP) to form geranyl diphosphate (GPP) and between IPP

38 two molecules of dimethylallyl diphosphate (DMAPP) to form lavandulyl diphosphate, a precursor to th

39 erase, which uses dimethylallyl diphosphate (DMAPP) to isopentenylate A residues adjacent to the anti

40 he C(5) substrate dimethylallyl diphosphate (DMAPP) to the C(15) product farnesyl diphosphate (FPP) b

41 ed derivatives of dimethylallyl diphosphate (DMAPP) useful for enzymological studies are reported.

42 ellular levels of dimethylallyl diphosphate (DMAPP), a central intermediate of isoprenoid metabolism

43 iphosphate (IPP), dimethylallyl diphosphate (DMAPP), geranyl diphosphate (GPP), farnesyl diphosphate

44 osphate (IPP) and dimethylallyl diphosphate (DMAPP), the basic building blocks of isoprenoid molecule

45 osphate (IPP) and dimethylallyl diphosphate (DMAPP), the basic five-carbon building blocks of isopren

46 osphate (IPP) and dimethylallyl diphosphate (DMAPP), the essential building blocks of isoprenoid comp

47 P) and its isomer dimethylallyl diphosphate (DMAPP), the more than 30 000 members of the isoprenoid f

48 n the presence of dimethylallyl diphosphate (DMAPP), the recombinant enzyme accepted very well simple

49 osphate (IPP) and dimethylallyl diphosphate (DMAPP), where it intersects with the mevalonate pathway

50 osphate (IPP) and dimethylallyl diphosphate (DMAPP), where the C3 methyl groups were replaced by chlo

51 P) and its isomer dimethylallyl diphosphate (DMAPP), which can be derived from the mevalonic acid (MV

52 osphate (IPP) and dimethylallyl diphosphate (DMAPP).

53 osphate (IPP) and dimethylallyl diphosphate (DMAPP).

54 osphate (IPP) and dimethylallyl diphosphate (DMAPP).

55 osphate (IPP) and dimethylallyl diphosphate (DMAPP).

56 ersion of IPP and dimethylallyl diphosphate (DMAPP).

57 osphate (IPP) and dimethylallyl diphosphate (DMAPP).

58 cleophilic isomer dimethylallyl diphosphate (DMAPP).

59 osphate (IPP) and dimethylallyl diphosphate (DMAPP).

60 tic production of dimethylallyl diphosphate (DMAPP).

61 ocarbon moiety of dimethylallyl diphosphate (DMAPP).

62 osphate (IPP) and dimethylallyl diphosphate (DMAPP).

63 te (IPP, C5) with dimethylallyl diphosphate (DMAPP, C5) and geranyl diphosphate (GPP, C10) to give (E

64 osphate (IPP) and dimethylallyl-diphosphate (DMAPP) precursors of isoprene.

65 ence alignment of 28 gene sequences encoding DMAPP-tRNA transferases from various organisms revealed

66 nd stereoselectivity and the need to exclude DMAPP from the IPP binding site.

67 Diene analogues for DMAPP (E-2-OPP and Z-2-OPP) and IPP (4-OPP) were synthes

68 because of the lack of a sensitive assay for DMAPP in plant tissues.

69 ity was strongly competitively inhibited for DMAPP by ATP and ADP (Kiapp = 0.06 microM), suggesting t

70 However, DMAPP was bound with a dissociation constant of 3.4 +/-

71 chemical quench experiments show no burst in DMAPP formation, suggesting that the rate determining st

72 at C3 in IPP and the Z-methyl group at C3 in DMAPP (3-OPP) and GPP (4-OPP), respectively.

73 al changes indicate that the binding of IPP, DMAPP, and a saturated analogue isopentyl diphosphate pr

74 The steady-state equilibrium ratio of IPP/DMAPP in the enzymatic reactions was approximately 1:7.

75 s by controlling the ratio of IP/DMAP to IPP/DMAPP.

76 purified tRNA modification enzymes, a Kmapp (DMAPP) = 632 nM, and a kcatapp = 0.44 s-1.

77 Substantial changes in k(cat), K(m)(DMAPP), and/or K(m)(RNA) were seen for several of the mu

78 k(as) = 6 x 10(3) M(-1) s(-1) for binding of DMAPP to E. coli IDI that is similar to rate constants d

79 determine the intracellular distribution of DMAPP in isoprene-emitting cottonwood (Populus deltoides

80 The assay is based on the hydrolysis of DMAPP in acid to the volatile hydrocarbon isoprene (2-me

81 zyme transferred the dimethylallyl moiety of DMAPP to A37, located adjacent to the anticodon in under

82 liyl diphosphate (MPP) from two molecules of DMAPP, and couples IPP to DMAPP to give GPP.

83 at most of the light-dependent production of DMAPP was chloroplastic in origin.

84 potential for light-dependent production of DMAPP.

85 n of the carbon-carbon double bond in IPP or DMAPP to form a tertiary carbocation, followed by deprot

86 the reduced enzyme was incubated with IPP or DMAPP.

87 BO emissions is in part due to controls over DMAPP production.

88 ate between the substrate (IPP) and product (DMAPP), indicating that the FMN cofactor must start and

89 phate (IPP) to dimethyl allyl pyrophosphate (DMAPP) and vice versa.

90 zes gamma,gamma-dimethylallyl pyrophosphate (DMAPP) and isopentenyl pyrophosphate (IPP) to all of the

91 oid moiety from dimethylallyl pyrophosphate (DMAPP) to the amino group of adenosine at position 37 of

92 sphate (IPP) to dimethylallyl pyrophosphate (DMAPP), a reaction with no net change in redox state of

93 phate (IPP) and dimethylallyl pyrophosphate (DMAPP), which are required to initiate the biosynthesis

94 Using a recent DMAPP assay developed in our laboratories, we report tha

95 ng substrate tRNA and the donating substrate DMAPP appear to enter the channel from opposite sides in

96 Affinity-tagged DMAPP-tRNA transferase containing a C-terminal tripeptid

97 is inhibited substantially in vivo and that DMAPP may bind to a conserved P-loop motif in this class

98 Evidence is presented to show that DMAPP is the major leaf metabolite giving rise to isopre

99 izes and a second site (S2) which houses the DMAPP nucleophile.

100 rmodified tRNA(Phe) used as substrate in the DMAPP-tRNA transferase-catalyzed reaction was isolated a

101 des) leaves; approximately 65% to 70% of the DMAPP recovered at midday occurred in the chloroplasts,

102 terminal tripeptide alpha-tubulin epitope to DMAPP-tRNA transferase did not affect the activity of th

103 The subsequent isomerization of IPP to DMAPP activates the five-carbon isoprene unit for subseq

104 m two molecules of DMAPP, and couples IPP to DMAPP to give GPP.

105 mining step in the forward direction (IPP to DMAPP) occurs prior to DMAPP formation.

106 the enzyme for multiple turnovers of IPP to DMAPP.

107 kely to catalyze the isomerization of IPP to DMAPP.

108 ard direction (IPP to DMAPP) occurs prior to DMAPP formation.

109 role in the deprotonation of IPP en route to DMAPP formation.

110 inetic constants were measured for wild-type DMAPP-tRNA transferase and the site-directed mutants usi

111 coexpressed chromosomally encoded wild-type DMAPP-tRNA transferase.

112 nsferase and the site-directed mutants using DMAPP and a 17-base RNA oligoribonucleotide correspondin

113 Initial screens using DMAPP and GPP as substrates indicated that two of the su

114 , and contains an allylic site (S1) in which DMAPP ionizes and a second site (S2) which houses the DM

115 Values of K(M)(3-ClIPP) (with DMAPP) and K(M)(3-ClDMAPP) (with IPP) were similar to th

116 analysis of the products from reactions with DMAPP in the presence of excess IPP and by comparing the