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1 complex with an inert thioether analogue of methylmalonyl CoA.
2 tion, has been solved bound to its substrate methylmalonyl-CoA.
3 ochemical selectivity of the enzyme for (2R)-methylmalonyl-CoA.
4 -TE does not catalyze the decarboxylation of methylmalonyl-CoA.
5 tibiotic erythromycin from propionyl-CoA and methylmalonyl-CoA.
6 l-CoA and propionyl-CoA over malonyl-CoA and methylmalonyl-CoA.
7 talyzes the conversion of propionyl-CoA to D-methylmalonyl-CoA.
8 fold increase in the K(M) for the substrate, methylmalonyl-CoA.
9 esis in Escherichia coli is the lack of (2S)-methylmalonyl-CoA, a common substrate of multimodular po
10 se (AT/DC) that derives propionyl-S-ACP from methylmalonyl-CoA, accounting for the missing link of th
11 ing in the EPR signals produced by [2'-(13)C]methylmalonyl-CoA and [2-(13)C]methylmalonyl-CoA as well
12 lonyl-CoA mutase in complexes with substrate methylmalonyl-CoA and inhibitors 2-carboxypropyl-CoA and
13 tify mutations in ACSF3, encoding a putative methylmalonyl-CoA and malonyl-CoA synthetase as a cause
15 he fumarate needed for alkane activation via methylmalonyl-CoA and predicted the capability for syntr
19 dependent decarboxylation of malonyl-CoA and methylmalonyl-CoA and the hydrolysis of CoA esters such
20 ependent on the enzymatic decarboxylation of methylmalonyl-CoA and transfer of the acyl chain within
21 acid, which is formed from the MCM substrate methylmalonyl-CoA and which inhibits succinate dehydroge
22 oxylated CoA thioester (e.g., malonyl-CoA or methylmalonyl-CoA) and an acyl carrier protein (ACP).
23 yn-(2S,3R)-2-methyl-3-hydroxypentanoate (6), methylmalonyl-CoA, and NADPH resulting in the exclusive
24 noyl-N-acetylcysteamine thioester (2b-SNAC), methylmalonyl-CoA, and NADPH with DEBS [KS6][AT6], DEBS
25 cubation of a mixture of propionyl-SNAC (4), methylmalonyl-CoA, and NADPH with the DEBS beta-ketoacyl
26 2S,3R)-2-methyl-3-hydroxypentanoyl-SNAC (5), methylmalonyl-CoA, and NADPH with the recombinant [KS6][
29 s isotopomer distributions of propionyl-CoA, methylmalonyl-CoA, and succinyl-CoA revealed that, in in
31 that ascomycin AT8 does not use malonyl- or methylmalonyl-CoA as a substrate in its native context.
34 l-pyrroline-5-carboxylate and malonyl-CoA or methylmalonyl-CoA as the CoA esters of (2S,5S)-5-carboxy
36 by [2'-(13)C]methylmalonyl-CoA and [2-(13)C]methylmalonyl-CoA as well as line narrowing resulting fr
37 coli strain produced both propionyl-CoA and methylmalonyl-CoA at intracellular levels similar to tho
39 Such multienzymes typically use malonyl and methylmalonyl-CoA building blocks for polyketide chain a
46 nucleophilic attack of the carboxyl group in methylmalonyl-CoA does not appear to depend on interacti
47 ethylmalonyl-CoA racemase reaction keeps the methylmalonyl-CoA enantiomers in isotopic equilibrium un
49 omerizations (glyoxalase I), epimerizations (methylmalonyl-CoA epimerase), oxidative cleavage of C-C
51 four extender units were known: malonyl-CoA, methylmalonyl-CoA, ethylmalonyl-CoA, and methoxymalonyl-
52 t elongation of the n-C20 acyl primer by one methylmalonyl-CoA extender unit was catalyzed by fatty a
55 Here we report a route for synthesizing (2S)-methylmalonyl-CoA from malonyl-CoA with a 3-hydroxypropi
56 y homogeneous synthase exhibits an intrinsic methylmalonyl-CoA hydrolase activity, which competes wit
57 simple precursors such as propionyl-CoA and methylmalonyl-CoA in a biosynthetic process that closely
59 h the cellular pool of propionate and, thus, methylmalonyl CoA increasing upon cholesterol metabolism
62 rboxylate group of the thioether analogue of methylmalonyl CoA is hydrogen bonded to the peptidic NH
64 Therefore, although neither malonyl-CoA nor methylmalonyl-CoA is a substrate for ascomycin AT8 in it
67 active site, the labile carboxylate group of methylmalonyl-CoA is stabilized by interaction with the
68 log of the natural ACP-bound substrate, with methylmalonyl-CoA (MM-CoA) in the absence of NADPH gave
69 Da hexamer that transfers carboxlylate from methylmalonyl-CoA (MM-CoA) to biotin; in turn, the bioti
71 o-crystallization with malonyl-CoA (MCoA) or methylmalonyl-CoA (MMCoA) led to partial turnover of the
76 he presence and absence of nucleotides) with methylmalonyl-CoA mutase (in the presence and absence of
77 significant amino acid sequence identity to methylmalonyl-CoA mutase (MCM) (40%) and isobutyryl-CoA
78 tive 5'-deoxyadenosylcobalamin cofactor onto methylmalonyl-CoA mutase (MCM) and precludes loading of
81 mans, deficiencies in coenzyme B12-dependent methylmalonyl-CoA mutase (MCM) lead to methylmalonyl aci
82 of bacterial and mitochondrial B12-dependent methylmalonyl-CoA mutase (MCM), HCM has a highly conserv
83 osylcobalamin (AdoCbl or coenzyme B(12)), to methylmalonyl-CoA mutase (MCM), resulting in holoenzyme
87 f metabolism caused by defective activity of methylmalonyl-CoA mutase (MUT) that exhibits multiorgan
88 ed by deficiency of the mitochondrial enzyme methylmalonyl-CoA mutase (MUT), is often complicated by
89 aciduria (MMAuria), caused by deficiency of methylmalonyl-CoA mutase (MUT), usually presents in the
92 We found that nitric oxide (NO) inhibits methylmalonyl-CoA mutase activity in rodent cell extract
93 r inhibiting cellular NO synthesis increased methylmalonyl-CoA mutase activity when measured subseque
94 Methylobacterium extorquens, which supports methylmalonyl-CoA mutase activity, serves dual functions
96 nction of two crucial enzymes, mitochondrial methylmalonyl-CoA mutase and cytosolic methionine syntha
97 cluding adenosylcobalamin (AdoCbl)-dependent methylmalonyl-CoA mutase and hydrogenase, and thus have
99 ich catalyze carbon skeleton rearrangements, methylmalonyl-CoA mutase and isobutyryl-CoA mutase (ICM)
101 The dissociation constant for binding of methylmalonyl-CoA mutase and MeaB ranges from 34 +/- 4 t
102 cs of interaction between the radical enzyme methylmalonyl-CoA mutase and MeaB, which are discussed.
103 on the kinetics of the reaction catalyzed by methylmalonyl-CoA mutase and on the thermodynamics of co
104 is to create the H610A and H610N variants of methylmalonyl-CoA mutase and report that both mutations
105 demonstrated that MeaB forms a complex with methylmalonyl-CoA mutase and stimulates in vitro mutase
107 ability of the double mutant (Y89F/R207Q) of methylmalonyl-CoA mutase as well as of the single mutant
114 he hypothesis that MeaB functions to protect methylmalonyl-CoA mutase from irreversible inactivation.
116 CoA, we inferred that conserved neighbors of methylmalonyl-CoA mutase genes and their human homologue
117 at were frequently arranged with prokaryotic methylmalonyl-CoA mutase genes, and that were of unknown
118 cobalamin-dependent methionine synthase and methylmalonyl-CoA mutase have revealed a striking confor
120 usly for the related Cbl-dependent isomerase methylmalonyl-CoA mutase indicate that a common mechanis
126 yadenosylcobalamin by adenosyltransferase to methylmalonyl-CoA mutase is gated by a small G protein,
128 alonyl-CoA supplied in vivo by the AtoAD and methylmalonyl-CoA mutase pathways, respectively, to prod
129 m under all conditions tested, and (iii) the methylmalonyl-CoA mutase reaction is reversible, but its
132 m a primary CH(3)- group in AdoCbl-dependent methylmalonyl-CoA mutase shows the enzymic and enzyme-fr
133 ism is demonstrated by a patient mutation in methylmalonyl-CoA mutase that does not impair the activi
134 The alignments allow the mutations of human methylmalonyl-CoA mutase to be mapped onto the structure
135 mutase and a recently characterized archaeal methylmalonyl-CoA mutase, allowed demonstration of its r
136 ction of the radical B(12)-dependent enzyme, methylmalonyl-CoA mutase, although its precise role is n
140 tion of Co-carbon bond homolysis rate in the methylmalonyl-CoA mutase-catalyzed reaction has been eva
157 e of the better characterized and homologous methylmalonyl-CoA mutase/G-protein chaperone system.
158 rward direction by reducing the ratio of apo-methylmalonyl-CoA mutase/holo-ATR required for delivery
161 four-gene operon that encodes homologues of methylmalonyl CoA mutases (Sbm) and acyl CoA transferase
165 which transfers the methylmalonyl moiety of methylmalonyl-CoA onto the phosphopantetheine arm of the
166 g only propionyl-CoA, and not malonyl-CoA, 2-methylmalonyl-CoA or acetyl-CoA, as the starter unit of
167 ive in MeaB and in the synthesis of either R-methylmalonyl-CoA or adenosylcobalamin indicates that Me
169 ic acid N-acetylcysteamine thioester (2) and methylmalonyl-CoA plus NADPH result in formation of a re
170 valine degradation, implicated in providing methylmalonyl-CoA precursors for many polyketide biosynt
171 aA gene product is significantly involved in methylmalonyl-CoA production in S. cinnamonensis and tha
172 In this report, we identify the human DL-methylmalonyl-CoA racemase gene by analyzing prokaryotic
173 ble only at low propionyl-CoA flux, (ii) the methylmalonyl-CoA racemase reaction keeps the methylmalo
175 vides the structural basis for engineering a methylmalonyl-CoA reductase applied for biotechnical pol
177 action by orienting the carboxylate group of methylmalonyl CoA so that it is orthogonal to the plane
178 placing the AT domain of this protein with a methylmalonyl-CoA specific AT domain from module 6 of th
182 ynthases that selectively use malonyl-CoA or methylmalonyl-CoA suggested that the acyltransferase (AT
183 lyketide synthase (PKS) used butyryl-CoA and methylmalonyl-CoA supplied in vivo by the AtoAD and meth
185 confer to synthases that normally do not use methylmalonyl-CoA the ability to incorporate methylmalon
186 propionyl-CoA as its substrate and produces methylmalonyl-CoA, the substrate for the biosyntheses of
188 thase (PKS) that catalyzes the conversion of methylmalonyl-CoA to narbonolide and 10-deoxymethynolide
190 alyzes the transfer of a carboxyl group from methylmalonyl-CoA to pyruvate to form propionyl-CoA and
191 lyzing the transfer of a carboxyl group from methylmalonyl-CoA to pyruvate to form propionyl-CoA and
192 lation reactions, transferring CO(2)(-) from methylmalonyl-CoA to pyruvate to yield propionyl-CoA and
193 lation reactions, transferring CO(2)(-) from methylmalonyl-CoA to pyruvate, yielding propionyl-CoA an
195 yl-CoA mutase catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA that uses reactive rad
206 EpoC transfers the methylmalonyl moiety from methylmalonyl-CoA to the holo HS-acyl carrier protein (A
207 t chimeric protein converted diketide 1 with methylmalonyl-CoA to triketide ketolactone 6 with improv
208 nthesis can be primed via decarboxylation of methylmalonyl-CoA; under these conditions the overall k(
209 ation of the n-C12 acyl primer mainly by one methylmalonyl-CoA unit was catalyzed by an E. coli fatty
210 ns of AT4 believed to confer specificity for methylmalonyl-CoA were mutated into the sequence seen in
212 hed that the decarboxylative condensation of methylmalonyl-CoA with S-propionyl-N-acetylcysteamine ca
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