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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)
7 reactive toward proton addition than IPP and DMAPP but have similar reactivities toward hydrogen atom
9 iate in the pathway, is converted to IPP and DMAPP by the consecutive action of the IspD-H proteins.
10 responsible for converting HMBPP to IPP and DMAPP in the ultimate step in the nonmevalonate pathway.
11 alone, indicating that the ratio of IPP and DMAPP produced via the DOXP pathway is influenced by Lyt
12 llular substrate in Synechocystis to IPP and DMAPP, overcoming flux limitations of the native MEP pat
14 s from the respective C5-precursors, IPP and DMAPP, whereas one isoprene unit in the ring E of 1 show
18 (with IPP) were similar to those for IPP and DMAPP; however, values of k(cat) for both analogues were
23 cific (13)C isotopic labeling exclusively at DMAPP-derived positions of MK-7 and demonstrate that IPP
25 ficult to study the relationship of cellular DMAPP levels to emission of these volatiles because of t
26 The midday concentration of chloroplastic DMAPP in cottonwood leaves is estimated to be 0.13 to 3.
29 ed with deuterium at the (E)-methyl group (d-DMAPP) and a 34% yield of IPP labeled with 1 mol of deut
32 l diphosphate:tRNA dimethylallyltransferase (DMAPP-tRNA transferase) catalyzes alkylation of the exoc
33 l diphosphate:tRNA dimethylallyltransferase (DMAPP-tRNA transferase) catalyzes the alkylation of the
34 l diphosphate:tRNA dimethylallyltransferase (DMAPP-tRNA transferase) catalyzes the first step in the
36 hosphate (IPP) to dimethylallyl diphosphate (DMAPP) in the mevalonate entry into the isoprenoid biosy
38 diphosphate (IPP):dimethylallyl diphosphate (DMAPP) isomerase (IDI-2) is a flavoenzyme that requires
39 en incubated with dimethylallyl diphosphate (DMAPP) or geranyl diphosphate (GPP) to give the correspo
40 osphate (IPP) and dimethylallyl diphosphate (DMAPP) to form geranyl diphosphate (GPP) and between IPP
41 two molecules of dimethylallyl diphosphate (DMAPP) to form lavandulyl diphosphate, a precursor to th
42 erase, which uses dimethylallyl diphosphate (DMAPP) to isopentenylate A residues adjacent to the anti
43 he C(5) substrate dimethylallyl diphosphate (DMAPP) to the C(15) product farnesyl diphosphate (FPP) b
44 ed derivatives of dimethylallyl diphosphate (DMAPP) useful for enzymological studies are reported.
45 ellular levels of dimethylallyl diphosphate (DMAPP), a central intermediate of isoprenoid metabolism
46 iphosphate (IPP), dimethylallyl diphosphate (DMAPP), geranyl diphosphate (GPP), farnesyl diphosphate
47 osphate (IPP) and dimethylallyl diphosphate (DMAPP), the basic building blocks of isoprenoid molecule
48 osphate (IPP) and dimethylallyl diphosphate (DMAPP), the basic five-carbon building blocks of isopren
49 osphate (IPP) and dimethylallyl diphosphate (DMAPP), the essential building blocks of isoprenoid comp
50 P) and its isomer dimethylallyl diphosphate (DMAPP), the more than 30 000 members of the isoprenoid f
51 n the presence of dimethylallyl diphosphate (DMAPP), the recombinant enzyme accepted very well simple
52 osphate (IPP) and dimethylallyl diphosphate (DMAPP), where it intersects with the mevalonate pathway
53 osphate (IPP) and dimethylallyl diphosphate (DMAPP), where the C3 methyl groups were replaced by chlo
54 P) and its isomer dimethylallyl diphosphate (DMAPP), which can be derived from the mevalonic acid (MV
66 te (IPP, C5) with dimethylallyl diphosphate (DMAPP, C5) and geranyl diphosphate (GPP, C10) to give (E
69 ence alignment of 28 gene sequences encoding DMAPP-tRNA transferases from various organisms revealed
73 ity was strongly competitively inhibited for DMAPP by ATP and ADP (Kiapp = 0.06 microM), suggesting t
75 chemical quench experiments show no burst in DMAPP formation, suggesting that the rate determining st
77 al changes indicate that the binding of IPP, DMAPP, and a saturated analogue isopentyl diphosphate pr
78 The steady-state equilibrium ratio of IPP/DMAPP in the enzymatic reactions was approximately 1:7.
81 introduction of this stable isotope-labeled DMAPP facilitates the tracking of DMAPP-derived metaboli
83 l-permeant, stable isotope-labeled analog of DMAPP that employs self-immolating esters to mask the be
84 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
85 determine the intracellular distribution of DMAPP in isoprene-emitting cottonwood (Populus deltoides
87 zyme transferred the dimethylallyl moiety of DMAPP to A37, located adjacent to the anticodon in under
93 pe-labeled DMAPP facilitates the tracking of DMAPP-derived metabolites in native biological contexts
94 n of the carbon-carbon double bond in IPP or DMAPP to form a tertiary carbocation, followed by deprot
97 non-volatile isoprenoids, but the plastidic DMAPP:IPP ratio is generally believed to be similar acro
98 ate between the substrate (IPP) and product (DMAPP), indicating that the FMN cofactor must start and
99 onstrate that (13)C-labeled, ester-protected DMAPP ((13)C(3) SIE-DMAPP) achieves significant incorpor
101 phate (DMAP) and dimethyallyl pyrophosphate (DMAPP) dependent UbiX enzymes, we reveal the first step,
102 zes gamma,gamma-dimethylallyl pyrophosphate (DMAPP) and isopentenyl pyrophosphate (IPP) to all of the
103 oid moiety from dimethylallyl pyrophosphate (DMAPP) to the amino group of adenosine at position 37 of
104 sphate (IPP) to dimethylallyl pyrophosphate (DMAPP), a reaction with no net change in redox state of
105 phate (IPP) and dimethylallyl pyrophosphate (DMAPP), which are required to initiate the biosynthesis
106 sphate (IPP) to dimethylallyl pyrophosphate (DMAPP), with volatile isoprenoids containing fewer isope
111 labeled, ester-protected DMAPP ((13)C(3) SIE-DMAPP) achieves significant incorporation into menaquino
112 ng substrate tRNA and the donating substrate DMAPP appear to enter the channel from opposite sides in
114 is inhibited substantially in vivo and that DMAPP may bind to a conserved P-loop motif in this class
118 rmodified tRNA(Phe) used as substrate in the DMAPP-tRNA transferase-catalyzed reaction was isolated a
119 des) leaves; approximately 65% to 70% of the DMAPP recovered at midday occurred in the chloroplasts,
120 terminal tripeptide alpha-tubulin epitope to DMAPP-tRNA transferase did not affect the activity of th
129 inetic constants were measured for wild-type DMAPP-tRNA transferase and the site-directed mutants usi
131 nsferase and the site-directed mutants using DMAPP and a 17-base RNA oligoribonucleotide correspondin
134 , and contains an allylic site (S1) in which DMAPP ionizes and a second site (S2) which houses the DM
136 analysis of the products from reactions with DMAPP in the presence of excess IPP and by comparing the