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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)
6                            Natively, IPP and DMAPP are generated by the mevalonate (MVA) and 2-C-meth
7 reactive toward proton addition than IPP and DMAPP but have similar reactivities toward hydrogen atom
8 eria, catalyzes the isomerization of IPP and DMAPP by a protonation-deprotonation mechanism.
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
13  are approximately 50-fold less than IPP and DMAPP, respectively.
14 s from the respective C5-precursors, IPP and DMAPP, whereas one isoprene unit in the ring E of 1 show
15 hibition of endogenous production of IPP and DMAPP.
16 r to those for chain elongation with IPP and DMAPP.
17 he enzyme-catalyzed isomerization of IPP and DMAPP.
18 (with IPP) were similar to those for IPP and DMAPP; however, values of k(cat) for both analogues were
19                          Thus, when ISPP and DMAPP were incubated with FPPase, GSPP accumulated and w
20        Michaelis constants for tRNA(Phe) and DMAPP are 96 +/- 11 nM and 3.2 +/- 0.5 microM, respectiv
21 ynthase were determined for L-tryptophan and DMAPP at 34 and 76 muM, respectively.
22 ulated from kinetic data of L-tryptophan and DMAPP.
23 cific (13)C isotopic labeling exclusively at DMAPP-derived positions of MK-7 and demonstrate that IPP
24 ze the isomerization of [(14)C]IPP to [(14)C]DMAPP.
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.
27                   Active recombinant E. coli DMAPP-tRNA transferase is monomeric.
28                                 In contrast, DMAPP did not bind to the enzyme in the absence of tRNA.
29 ed with deuterium at the (E)-methyl group (d-DMAPP) and a 34% yield of IPP labeled with 1 mol of deut
30 ial product of the IDI-catalyzed reaction (d-DMAPP) is slower than its conversion to d-IPP.
31 uction also exhibit elevated light-dependent DMAPP production, ranging from 110% to 1,063%.
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
35 hosphate (IPP) to dimethylallyl diphosphate (DMAPP) and then to geranyl diphosphate (GPP).
36 hosphate (IPP) to dimethylallyl diphosphate (DMAPP) in the mevalonate entry into the isoprenoid biosy
37 he substrates for dimethylallyl diphosphate (DMAPP) IPT activity.
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
55 osphate (IPP) and dimethylallyl diphosphate (DMAPP).
56 osphate (IPP) and dimethylallyl diphosphate (DMAPP).
57 hosphate (IPP) or dimethylallyl diphosphate (DMAPP).
58 osphate (IPP) and dimethylallyl diphosphate (DMAPP).
59 osphate (IPP) and dimethylallyl diphosphate (DMAPP).
60 osphate (IPP) and dimethylallyl diphosphate (DMAPP).
61 ersion of IPP and dimethylallyl diphosphate (DMAPP).
62 cleophilic isomer dimethylallyl diphosphate (DMAPP).
63 osphate (IPP) and dimethylallyl diphosphate (DMAPP).
64 tic production of dimethylallyl diphosphate (DMAPP).
65 ocarbon moiety of dimethylallyl diphosphate (DMAPP).
66 te (IPP, C5) with dimethylallyl diphosphate (DMAPP, C5) and geranyl diphosphate (GPP, C10) to give (E
67 osphate (IPP) and dimethylallyl-diphosphate (DMAPP) precursors of isoprene.
68 hate [GPP] versus dimethylallyl diphosphate [DMAPP]) with a single amino acid change.
69 ence alignment of 28 gene sequences encoding DMAPP-tRNA transferases from various organisms revealed
70 nd stereoselectivity and the need to exclude DMAPP from the IPP binding site.
71                          Diene analogues for DMAPP (E-2-OPP and Z-2-OPP) and IPP (4-OPP) were synthes
72 because of the lack of a sensitive assay for DMAPP in plant tissues.
73 ity was strongly competitively inhibited for DMAPP by ATP and ADP (Kiapp = 0.06 microM), suggesting t
74                                     However, DMAPP was bound with a dissociation constant of 3.4 +/-
75 chemical quench experiments show no burst in DMAPP formation, suggesting that the rate determining st
76 at C3 in IPP and the Z-methyl group at C3 in DMAPP (3-OPP) and GPP (4-OPP), respectively.
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.
79 s by controlling the ratio of IP/DMAP to IPP/DMAPP.
80 purified tRNA modification enzymes, a Kmapp (DMAPP) = 632 nM, and a kcatapp = 0.44 s-1.
81  introduction of this stable isotope-labeled DMAPP facilitates the tracking of DMAPP-derived metaboli
82          Substantial changes in k(cat), K(m)(DMAPP), and/or K(m)(RNA) were seen for several of the mu
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
86      The assay is based on the hydrolysis of DMAPP in acid to the volatile hydrocarbon isoprene (2-me
87 zyme transferred the dimethylallyl moiety of DMAPP to A37, located adjacent to the anticodon in under
88 liyl diphosphate (MPP) from two molecules of DMAPP, and couples IPP to DMAPP to give GPP.
89 at most of the light-dependent production of DMAPP was chloroplastic in origin.
90  potential for light-dependent production of DMAPP.
91  isotopic labeling of downstream products of DMAPP in Bacillus subtilis.
92        Here we demonstrate that the ratio of DMAPP:IPP produced by hydroxymethylbutenyl diphosphate r
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
95 the reduced enzyme was incubated with IPP or DMAPP.
96 BO emissions is in part due to controls over DMAPP production.
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
100 phate (IPP) to dimethyl allyl pyrophosphate (DMAPP) and vice versa.
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
107 phate (IPP) and dimethylallyl pyrophosphate (DMAPP).
108 d/or its isomer dimethylallyl pyrophosphate (DMAPP).
109 phate (IPP) and dimethylallyl pyrophosphate (DMAPP).
110                               Using a recent DMAPP assay developed in our laboratories, we report tha
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
113                              Affinity-tagged DMAPP-tRNA transferase containing a C-terminal tripeptid
114  is inhibited substantially in vivo and that DMAPP may bind to a conserved P-loop motif in this class
115           Evidence is presented to show that DMAPP is the major leaf metabolite giving rise to isopre
116                                          The DMAPP:IPP ratio could affect the balance between volatil
117 izes and a second site (S2) which houses the DMAPP nucleophile.
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
121       The subsequent isomerization of IPP to DMAPP activates the five-carbon isoprene unit for subseq
122 m two molecules of DMAPP, and couples IPP to DMAPP to give GPP.
123 mining step in the forward direction (IPP to DMAPP) occurs prior to DMAPP formation.
124  the enzyme for multiple turnovers of IPP to DMAPP.
125 kely to catalyze the isomerization of IPP to DMAPP.
126 ard direction (IPP to DMAPP) occurs prior to DMAPP formation.
127 role in the deprotonation of IPP en route to DMAPP formation.
128                          Finally, we tracked DMAPP incorporation during the transition from vegetativ
129 inetic constants were measured for wild-type DMAPP-tRNA transferase and the site-directed mutants usi
130  coexpressed chromosomally encoded wild-type DMAPP-tRNA transferase.
131 nsferase and the site-directed mutants using DMAPP and a 17-base RNA oligoribonucleotide correspondin
132                        Initial screens using DMAPP and GPP as substrates indicated that two of the su
133 verexpression enables B. subtilis to utilize DMAPP as its sole isoprenoid source.
134 , and contains an allylic site (S1) in which DMAPP ionizes and a second site (S2) which houses the DM
135                Values of K(M)(3-ClIPP) (with DMAPP) and K(M)(3-ClDMAPP) (with IPP) were similar to th
136 analysis of the products from reactions with DMAPP in the presence of excess IPP and by comparing the

 
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