ライフサイエンスコーパス: methylmalonyl

1 e human adenosyltransferase (hATR) result in methylmalonyl aciduria (MMA), a rare but life-threatenin

2 n is altered in cell lines derived from cblB methylmalonyl aciduria patients compared with cell lines

3 ndent methylmalonyl-CoA mutase (MCM) lead to methylmalonyl aciduria, a rare disease that is often fat

4 hat inherited defects in this enzyme lead to methylmalonyl aciduria, but the corresponding ATR gene h

5 the human ATR gene identified here result in methylmalonyl aciduria.

6 rent ACP specificity, catalyzing cleavage of methylmalonyl-ACP from both AT(L)-ACP(L) (k(cat)/K(m) 3.

7 comparable efficiency regardless of whether methylmalonyl-ACP or malonyl-ACP were the nucleophilic s

8 ys and a range of acyl-ACP, malonyl-ACP, and methylmalonyl-ACP substrates derived from either PikAIII

9 yketide biosynthesis, extender units such as methylmalonyl acyl carrier protein (ACP) may prematurely

10 In the presence of similar concentrations of methylmalonyl- and ethylmalonyl-CoA substrates, DEBS syn

11 ed specificity of the loading AT domain, the methylmalonyl- and malonyl-specific AT domains had high

12 ence of 1,1'-carbonyldiimidazole, or ethyl-2-methylmalonyl chloride (28b) under basic conditions to a

13 CarB was also shown to accept methylmalonyl CoA as a substrate to form 6-methyl-(2S,5S

14 The molecular structure of methylmalonyl CoA decarboxylase (MMCD), a newly defined

15 The identification of YgfG as methylmalonyl CoA decarboxylase expands the range of rea

16 We have determined that YgfG is methylmalonyl CoA decarboxylase, YgfH is propionyl CoA:s

17 h the cellular pool of propionate and, thus, methylmalonyl CoA increasing upon cholesterol metabolism

18 rboxylate group of the thioether analogue of methylmalonyl CoA is hydrogen bonded to the peptidic NH

19 the vitamin B12 (cobalamin)-dependent enzyme methylmalonyl CoA mutase.

20 yl CoA:succinate CoA transferase, and Sbm is methylmalonyl CoA mutase.

21 four-gene operon that encodes homologues of methylmalonyl CoA mutases (Sbm) and acyl CoA transferase

22 action by orienting the carboxylate group of methylmalonyl CoA so that it is orthogonal to the plane

23 All 12 CoA's (CoASH, HMG CoA, methylmalonyl CoA, succinyl CoA, methylcrotonyl CoA, iso

24 complex with an inert thioether analogue of methylmalonyl CoA.

25 iciency in the enzymes P-CoA carboxylase and methylmalonyl-CoA (M-CoA) mutase, respectively.

26 log of the natural ACP-bound substrate, with methylmalonyl-CoA (MM-CoA) in the absence of NADPH gave

27 Da hexamer that transfers carboxlylate from methylmalonyl-CoA (MM-CoA) to biotin; in turn, the bioti

28 ate reasonably well with those predicted for methylmalonyl-CoA (mMCoA) ATs.

29 o-crystallization with malonyl-CoA (MCoA) or methylmalonyl-CoA (MMCoA) led to partial turnover of the

30 zes the transfer of a carboxylate group from methylmalonyl-CoA (MMCoA) to pyruvate.

31 Subsequent binding of methylmalonyl-CoA (or CoA) promotes cob(II)alamin off-lo

32 this problem, we have synthesized a panel of methylmalonyl-CoA analogs with the carboxylate represent

33 ing in the EPR signals produced by [2'-(13)C]methylmalonyl-CoA and [2-(13)C]methylmalonyl-CoA as well

34 lonyl-CoA mutase in complexes with substrate methylmalonyl-CoA and inhibitors 2-carboxypropyl-CoA and

35 tify mutations in ACSF3, encoding a putative methylmalonyl-CoA and malonyl-CoA synthetase as a cause

36 etide lactone required the presence of (2RS)-methylmalonyl-CoA and NADPH.

37 he fumarate needed for alkane activation via methylmalonyl-CoA and predicted the capability for syntr

38 Methylmalonyl-CoA and succinyl-CoA are hydrolyzed and th

39 -CoA mutase catalyzes the interconversion of methylmalonyl-CoA and succinyl-CoA.

40 MCM interconverts (2R)-methylmalonyl-CoA and succinyl-CoA.

41 dependent decarboxylation of malonyl-CoA and methylmalonyl-CoA and the hydrolysis of CoA esters such

42 ependent on the enzymatic decarboxylation of methylmalonyl-CoA and transfer of the acyl chain within

43 acid, which is formed from the MCM substrate methylmalonyl-CoA and which inhibits succinate dehydroge

44 that ascomycin AT8 does not use malonyl- or methylmalonyl-CoA as a substrate in its native context.

45 rified sacogolassan protein EcPKS1 uses only methylmalonyl-CoA as a substrate, otherwise unknown in a

46 ed to enable the loading AT domain to accept methylmalonyl-CoA as an alternative substrate.

47 etylcysteamine-activated diketides and (14)C-methylmalonyl-CoA as substrates.

48 l-pyrroline-5-carboxylate and malonyl-CoA or methylmalonyl-CoA as the CoA esters of (2S,5S)-5-carboxy

49 erate triketide lactone products using (14)C-methylmalonyl-CoA as the sole substrate.

50 by [2'-(13)C]methylmalonyl-CoA and [2-(13)C]methylmalonyl-CoA as well as line narrowing resulting fr

51 coli strain produced both propionyl-CoA and methylmalonyl-CoA at intracellular levels similar to tho

52 s from Streptomyces coelicolor, which enable methylmalonyl-CoA biosynthesis.

53 Such multienzymes typically use malonyl and methylmalonyl-CoA building blocks for polyketide chain a

54 f isobutyryl-coenzyme A (isobutyryl-CoA) and methylmalonyl-CoA catalysed by a 3-ketoacyl-(acyl carrie

55 The apparent K(m) for (2S)-methylmalonyl-CoA consumption by DEBS 1+TE is 24 microM.

56 Structures of Escherichia coli methylmalonyl-CoA decarboxylase in complex with our anal

57 ncluding enoyl-CoA hydratase (crotonase) and methylmalonyl-CoA decarboxylase.

58 yl-CoA and propionyl-CoA carboxylases and of methylmalonyl-CoA decarboxylase.

59 nucleophilic attack of the carboxyl group in methylmalonyl-CoA does not appear to depend on interacti

60 ethylmalonyl-CoA racemase reaction keeps the methylmalonyl-CoA enantiomers in isotopic equilibrium un

61 ce; overexpression of NADH dehydrogenase and methylmalonyl-CoA epimerase improved PA tolerance.

62 omerizations (glyoxalase I), epimerizations (methylmalonyl-CoA epimerase), oxidative cleavage of C-C

63 ng glyoxalase I, extradiol dioxygenases, and methylmalonyl-CoA epimerase.

64 t elongation of the n-C20 acyl primer by one methylmalonyl-CoA extender unit was catalyzed by fatty a

65 one propionyl-CoA starter unit and six (2S)-methylmalonyl-CoA extender units.

66 S do not influence epimerization of the (2S)-methylmalonyl-CoA extender units.

67 Here we report a route for synthesizing (2S)-methylmalonyl-CoA from malonyl-CoA with a 3-hydroxypropi

68 y homogeneous synthase exhibits an intrinsic methylmalonyl-CoA hydrolase activity, which competes wit

69 We find that metabolic deficiency of methylmalonyl-CoA impedes the growth of PDIM-producing b

70 simple precursors such as propionyl-CoA and methylmalonyl-CoA in a biosynthetic process that closely

71 he component activities show selectivity for methylmalonyl-CoA in any biological system.

72 already contained methyl-branched FAs due to methylmalonyl-CoA incorporation, but these FAs were only

73 0-kDa protein inhibited the incorporation of methylmalonyl-CoA into fatty acids by SMAS.

74 methylmalonyl-CoA the ability to incorporate methylmalonyl-CoA into fatty acids.

75 is 0.84 min-1, and the apparent Km for (2RS)-methylmalonyl-CoA is 17 microM.

76 Therefore, although neither malonyl-CoA nor methylmalonyl-CoA is a substrate for ascomycin AT8 in it

77 Methylmalonyl-CoA is M3 and M2 labeled, reflecting rever

78 Decarboxylation of methylmalonyl-CoA is negligible in the presence of satur

79 active site, the labile carboxylate group of methylmalonyl-CoA is stabilized by interaction with the

80 Inherited defects in the gene for methylmalonyl-CoA mutase (EC 5.4.99.2) result in the mut

81 he presence and absence of nucleotides) with methylmalonyl-CoA mutase (in the presence and absence of

82 significant amino acid sequence identity to methylmalonyl-CoA mutase (MCM) (40%) and isobutyryl-CoA

83 tive 5'-deoxyadenosylcobalamin cofactor onto methylmalonyl-CoA mutase (MCM) and precludes loading of

84 tive, itaconyl-CoA, inhibits B(12)-dependent methylmalonyl-CoA mutase (MCM) by an unknown mechanism.

85 The methylmalonyl-CoA mutase (MCM) cDNA was highly expressed

86 Within this family, methylmalonyl-CoA mutase (MCM) is the best studied and i

87 mans, deficiencies in coenzyme B12-dependent methylmalonyl-CoA mutase (MCM) lead to methylmalonyl aci

88 of bacterial and mitochondrial B12-dependent methylmalonyl-CoA mutase (MCM), HCM has a highly conserv

89 osylcobalamin (AdoCbl or coenzyme B(12)), to methylmalonyl-CoA mutase (MCM), resulting in holoenzyme

90 he delivery of adenosylcobalamin (AdoCbl) to methylmalonyl-CoA mutase (MCM), the only AdoCbl-dependen

91 tion of 5'-deoxyadenosyl cobalamin-dependent methylmalonyl-CoA mutase (MCM).

92 so serves as an escort, delivering AdoCbl to methylmalonyl-CoA mutase (MCM).

93 Methylmalonyl-CoA mutase (MMCM) is an enzyme that utiliz

94 Our AAV vector was designed to insert a methylmalonyl-CoA mutase (MMUT) transgene into the 3' en

95 In these cells, the B(12)-dependent enzyme, methylmalonyl-CoA mutase (MMUT), plays a central role in

96 delivery and repair of B(12)-dependent human methylmalonyl-CoA mutase (MMUT).

97 oxidation-like pathways as well as inhibited methylmalonyl-CoA mutase (MUT) at lower doses.

98 L-Methylmalonyl-CoA mutase (MUT) is an adenosylcobalamin (

99 f metabolism caused by defective activity of methylmalonyl-CoA mutase (MUT) that exhibits multiorgan

100 ed by deficiency of the mitochondrial enzyme methylmalonyl-CoA mutase (MUT), is often complicated by

101 aciduria (MMAuria), caused by deficiency of methylmalonyl-CoA mutase (MUT), usually presents in the

102 inhibitor of the mitochondrial B12-dependent methylmalonyl-CoA mutase (MUT).

103 Methylmalonyl-CoA mutase accelerates the rate of Co-C bo

104 We found that nitric oxide (NO) inhibits methylmalonyl-CoA mutase activity in rodent cell extract

105 r inhibiting cellular NO synthesis increased methylmalonyl-CoA mutase activity when measured subseque

106 Methylobacterium extorquens, which supports methylmalonyl-CoA mutase activity, serves dual functions

107 nt activity of propionyl-CoA carboxylase and methylmalonyl-CoA mutase and are life-threatening condit

108 In the presence of methylmalonyl-CoA mutase and ATP, AdoCbl is transferred

109 nction of two crucial enzymes, mitochondrial methylmalonyl-CoA mutase and cytosolic methionine syntha

110 cluding adenosylcobalamin (AdoCbl)-dependent methylmalonyl-CoA mutase and hydrogenase, and thus have

111 In contrast, trans ligand effects in methylmalonyl-CoA mutase and indeed the significance of

112 ich catalyze carbon skeleton rearrangements, methylmalonyl-CoA mutase and isobutyryl-CoA mutase (ICM)

113 However, both methylmalonyl-CoA mutase and isobutyryl-CoA mutase, whic

114 The dissociation constant for binding of methylmalonyl-CoA mutase and MeaB ranges from 34 +/- 4 t

115 cs of interaction between the radical enzyme methylmalonyl-CoA mutase and MeaB, which are discussed.

116 impaired activity of the downstream enzymes, methylmalonyl-CoA mutase and methionine synthase.

117 on the kinetics of the reaction catalyzed by methylmalonyl-CoA mutase and on the thermodynamics of co

118 is to create the H610A and H610N variants of methylmalonyl-CoA mutase and report that both mutations

119 demonstrated that MeaB forms a complex with methylmalonyl-CoA mutase and stimulates in vitro mutase

120 Thus, NO inhibition of methylmalonyl-CoA mutase appeared to be from the reactio

121 ability of the double mutant (Y89F/R207Q) of methylmalonyl-CoA mutase as well as of the single mutant

122 Methylmalonyl-CoA mutase belongs to the class of adenosy

123 The inhibition of methylmalonyl-CoA mutase by NO was likely of physiologic

124 Methylmalonyl-CoA mutase catalyzes the adenosylcobalamin

125 Adenosylcobalamin-dependent methylmalonyl-CoA mutase catalyzes the interconversion o

126 Methylmalonyl-CoA mutase catalyzes the isomerization of

127 Methylmalonyl-CoA mutase catalyzes the isomerization of

128 el with samples from various mouse models of methylmalonyl-CoA mutase deficiency.

129 he hypothesis that MeaB functions to protect methylmalonyl-CoA mutase from irreversible inactivation.

130 MeaB and methylmalonyl-CoA mutase from M. extorquens were cloned

131 CoA, we inferred that conserved neighbors of methylmalonyl-CoA mutase genes and their human homologue

132 at were frequently arranged with prokaryotic methylmalonyl-CoA mutase genes, and that were of unknown

133 cobalamin-dependent methionine synthase and methylmalonyl-CoA mutase have revealed a striking confor

134 X-ray crystal structures of methylmalonyl-CoA mutase in complexes with substrate met

135 usly for the related Cbl-dependent isomerase methylmalonyl-CoA mutase indicate that a common mechanis

136 Methylmalonyl-CoA mutase is a key enzyme in intermediary

137 Methylmalonyl-CoA mutase is a member of the family of co

138 Methylmalonyl-CoA mutase is an 5'-adenosylcobalamin (Ado

139 Methylmalonyl-CoA mutase is an adenosylcobalamin (AdoCbl

140 Methylmalonyl-CoA mutase is an adenosylcobalamin-depende

141 yadenosylcobalamin by adenosyltransferase to methylmalonyl-CoA mutase is gated by a small G protein,

142 This study shows that methylmalonyl-CoA mutase is induced by several stresses,

143 alonyl-CoA supplied in vivo by the AtoAD and methylmalonyl-CoA mutase pathways, respectively, to prod

144 m under all conditions tested, and (iii) the methylmalonyl-CoA mutase reaction is reversible, but its

145 This portion of the methylmalonyl-CoA mutase sequence can be aligned with re

146 ace of the protein where its partner protein methylmalonyl-CoA mutase should bind.

147 m a primary CH(3)- group in AdoCbl-dependent methylmalonyl-CoA mutase shows the enzymic and enzyme-fr

148 ism is demonstrated by a patient mutation in methylmalonyl-CoA mutase that does not impair the activi

149 The alignments allow the mutations of human methylmalonyl-CoA mutase to be mapped onto the structure

150 mutase and a recently characterized archaeal methylmalonyl-CoA mutase, allowed demonstration of its r

151 ction of the radical B(12)-dependent enzyme, methylmalonyl-CoA mutase, although its precise role is n

152 enosylcobalamin (AdoCbl) to AdoCbl-dependent methylmalonyl-CoA mutase, an essential metabolic enzyme.

153 We show that methylmalonyl-CoA mutase, an R-specific crotonase, isobu

154 sential cofactor for methionine synthase and methylmalonyl-CoA mutase, but it must first undergo chem

155 ation of the enzymes methionine synthase and methylmalonyl-CoA mutase, disrupting gene expression and

156 adenosylcobalamin (AdoCbl)-dependent enzyme, methylmalonyl-CoA mutase, has been studied.

157 he essential enzymes methionine synthase and methylmalonyl-CoA mutase, respectively.

158 rone that escorts AdoCbl, transferring it to methylmalonyl-CoA mutase, which is important in propiona

159 tion of Co-carbon bond homolysis rate in the methylmalonyl-CoA mutase-catalyzed reaction has been eva

160 ct a qualitative free energy profile for the methylmalonyl-CoA mutase-catalyzed reaction.

161 ion of the active site residue, R207, in the methylmalonyl-CoA mutase-catalyzed reaction.

162 osylcobalamin but due to an inactive form of methylmalonyl-CoA mutase.

163 M3 and M2 labeled, reflecting reversal of S-methylmalonyl-CoA mutase.

164 ted with the homolysis reaction catalyzed by methylmalonyl-CoA mutase.

165 2-dependent enzymes, methionine synthase and methylmalonyl-CoA mutase.

166 cofactor required by methionine synthase and methylmalonyl-CoA mutase.

167 be a significant contributor to catalysis by methylmalonyl-CoA mutase.

168 ect residues in the C-terminal region of the methylmalonyl-CoA mutase.

169 um extorquens MeaB, which is a chaperone for methylmalonyl-CoA mutase.

170 dent target enzymes, methionine synthase and methylmalonyl-CoA mutase.

171 rotein interaction with its partner protein, methylmalonyl-CoA mutase.

172 n and assembly of the B(12)-dependent enzyme methylmalonyl-CoA mutase.

173 eaction catalyzed by the radical B12 enzyme, methylmalonyl-CoA mutase.

174 hich is stimulated approximately 100-fold by methylmalonyl-CoA mutase.

175 product Co2+ Cbl) is modulated by the enzyme methylmalonyl-CoA mutase.

176 e of the better characterized and homologous methylmalonyl-CoA mutase/G-protein chaperone system.

177 rward direction by reducing the ratio of apo-methylmalonyl-CoA mutase/holo-ATR required for delivery

178 Because methylmalonyl-CoA mutases are involved in the metabolism

179 dicted gene product showed 35% identity with methylmalonyl-CoA mutases from various sources.

180 oop GTPase and are currently misannotated as methylmalonyl-CoA mutases.

181 which transfers the methylmalonyl moiety of methylmalonyl-CoA onto the phosphopantetheine arm of the

182 g only propionyl-CoA, and not malonyl-CoA, 2-methylmalonyl-CoA or acetyl-CoA, as the starter unit of

183 ive in MeaB and in the synthesis of either R-methylmalonyl-CoA or adenosylcobalamin indicates that Me

184 the KS domains of MAS showed selectivity for methylmalonyl-CoA over malonyl-CoA.

185 ic acid N-acetylcysteamine thioester (2) and methylmalonyl-CoA plus NADPH result in formation of a re

186 valine degradation, implicated in providing methylmalonyl-CoA precursors for many polyketide biosynt

187 aA gene product is significantly involved in methylmalonyl-CoA production in S. cinnamonensis and tha

188 In this report, we identify the human DL-methylmalonyl-CoA racemase gene by analyzing prokaryotic

189 ble only at low propionyl-CoA flux, (ii) the methylmalonyl-CoA racemase reaction keeps the methylmalo

190 H0272 and its human homologue both encode DL-methylmalonyl-CoA racemases.

191 vides the structural basis for engineering a methylmalonyl-CoA reductase applied for biotechnical pol

192 These results show methylmalonyl-CoA selectivity for the AT and KS domains

193 placing the AT domain of this protein with a methylmalonyl-CoA specific AT domain from module 6 of th

194 This led to engineering of the methylmalonyl-CoA specificity of both modules and invers

195 ynthases that selectively use malonyl-CoA or methylmalonyl-CoA suggested that the acyltransferase (AT

196 lyketide synthase (PKS) used butyryl-CoA and methylmalonyl-CoA supplied in vivo by the AtoAD and meth

197 RpPat failed to acetylate the methylmalonyl-CoA synthetase of this bacterium (hereafte

198 confer to synthases that normally do not use methylmalonyl-CoA the ability to incorporate methylmalon

199 thase (PKS) that catalyzes the conversion of methylmalonyl-CoA to narbonolide and 10-deoxymethynolide

200 nthesis by catalyzing the decarboxylation of methylmalonyl-CoA to produce propionyl-CoA.

201 alyzes the transfer of a carboxyl group from methylmalonyl-CoA to pyruvate to form propionyl-CoA and

202 lyzing the transfer of a carboxyl group from methylmalonyl-CoA to pyruvate to form propionyl-CoA and

203 lation reactions, transferring CO(2)(-) from methylmalonyl-CoA to pyruvate to yield propionyl-CoA and

204 lation reactions, transferring CO(2)(-) from methylmalonyl-CoA to pyruvate, yielding propionyl-CoA an

205 product radical during the rearrangement of methylmalonyl-CoA to succinyl-CoA is unknown.

206 yl-CoA mutase catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA that uses reactive rad

207 mutase (MCM) catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA using 5'-deoxyadenosyl

208 somerases and catalyzes the rearrangement of methylmalonyl-CoA to succinyl-CoA.

209 t enzyme that catalyzes the rearrangement of methylmalonyl-CoA to succinyl-CoA.

210 t enzyme that catalyzes the rearrangement of methylmalonyl-CoA to succinyl-CoA.

211 rases and catalyzes the 1,2-rearrangement of methylmalonyl-CoA to succinyl-CoA.

212 zyme that catalyzes the 1,2 rearrangement of methylmalonyl-CoA to succinyl-CoA.

213 enzyme that catalyzes the isomerization of L-methylmalonyl-CoA to succinyl-CoA.

214 yl-CoA mutase catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA.

215 sylcobalamin-dependent rearrangement of (2R)-methylmalonyl-CoA to succinyl-CoA.

216 ompounds because of the inability to convert methylmalonyl-CoA to succinyl-CoA.

217 l) cofactor to catalyze the rearrangement of methylmalonyl-CoA to succinyl-CoA.

218 EpoC transfers the methylmalonyl moiety from methylmalonyl-CoA to the holo HS-acyl carrier protein (A

219 t chimeric protein converted diketide 1 with methylmalonyl-CoA to triketide ketolactone 6 with improv

220 ation of the n-C12 acyl primer mainly by one methylmalonyl-CoA unit was catalyzed by an E. coli fatty

221 ns of AT4 believed to confer specificity for methylmalonyl-CoA were mutated into the sequence seen in

222 SMAS utilizes methylmalonyl-CoA with C12 to C20 acyl-CoA as primers an

223 hed that the decarboxylative condensation of methylmalonyl-CoA with S-propionyl-N-acetylcysteamine ca

224 oxylated CoA thioester (e.g., malonyl-CoA or methylmalonyl-CoA) and an acyl carrier protein (ACP).

225 The methylmalonyl coenzyme A (methylmalonyl-CoA)-specific acyltransferase (AT) domains

226 esis in Escherichia coli is the lack of (2S)-methylmalonyl-CoA, a common substrate of multimodular po

227 te, and the Rv0158 protein directly binds to methylmalonyl-CoA, a key intermediate in propionate cata

228 se (AT/DC) that derives propionyl-S-ACP from methylmalonyl-CoA, accounting for the missing link of th

229 yn-(2S,3R)-2-methyl-3-hydroxypentanoate (6), methylmalonyl-CoA, and NADPH resulting in the exclusive

230 noyl-N-acetylcysteamine thioester (2b-SNAC), methylmalonyl-CoA, and NADPH with DEBS [KS6][AT6], DEBS

231 cubation of a mixture of propionyl-SNAC (4), methylmalonyl-CoA, and NADPH with the DEBS beta-ketoacyl

232 2S,3R)-2-methyl-3-hydroxypentanoyl-SNAC (5), methylmalonyl-CoA, and NADPH with the recombinant [KS6][

233 of reactions that require benzoate, Mg.ATP, methylmalonyl-CoA, and NADPH.

234 ss isotopomer distribution of propionyl-CoA, methylmalonyl-CoA, and succinyl-CoA in tissues.

235 s isotopomer distributions of propionyl-CoA, methylmalonyl-CoA, and succinyl-CoA revealed that, in in

236 four extender units were known: malonyl-CoA, methylmalonyl-CoA, ethylmalonyl-CoA, and methoxymalonyl-

237 propionyl-CoA as its substrate and produces methylmalonyl-CoA, the substrate for the biosyntheses of

238 In the presence of [CD3]methylmalonyl-CoA, this rate decreases to 28 +/- 2 s(-1)

239 thesis pathway and the vitamin B12-dependent methylmalonyl-CoA-mutase MutAB.

240 sets showed cystathionine beta synthase and methylmalonyl-CoA-mutase to be common to 3 out of 4 data

241 rk, to investigate the initial stages of the methylmalonyl-CoA-mutase-catalyzed reaction.

242 When AT8 was replaced with methylmalonyl-CoA-specific AT domains, the strains produ

243 fold increase in the K(M) for the substrate, methylmalonyl-CoA.

244 tion, has been solved bound to its substrate methylmalonyl-CoA.

245 ochemical selectivity of the enzyme for (2R)-methylmalonyl-CoA.

246 -TE does not catalyze the decarboxylation of methylmalonyl-CoA.

247 tibiotic erythromycin from propionyl-CoA and methylmalonyl-CoA.

248 l-CoA and propionyl-CoA over malonyl-CoA and methylmalonyl-CoA.

249 talyzes the conversion of propionyl-CoA to D-methylmalonyl-CoA.

250 nthesis can be primed via decarboxylation of methylmalonyl-CoA; under these conditions the overall k(

251 established that multifunctional enzymes use methylmalonyl coenzyme A (CoA) as the substrate to gener

252 The methylmalonyl coenzyme A (methylmalonyl-CoA)-specific ac

253 lative levels of the biosynthetic precursors methylmalonyl-coenzyme A (CoA) (monensin A and monensin

254 Human methylmalonyl-Coenzyme A (CoA) mutase (MCM) catalyzes th

255 Both malonyl-coenzyme A (MCoA) and methylmalonyl-coenzyme A (mMCoA) are substrates for chai

256 ders, due to deficiency of the mitochondrial methylmalonyl-coenzyme A mutase (MMUT).

257 yze carbon skeleton rearrangement, for which methylmalonyl-coenzyme A mutase is the prototype, also b

258 to the apoenzymes of methionine synthase and methylmalonyl-coenzyme A mutase: The dimethylbenzimidazo

259 in-dependent enzymes, methionine synthase or methylmalonyl-coenzyme A mutase; however, it did inhibit

260 de synthases likely is to act as malonyl, or methylmalonyl, decarboxylases that provide a source of p

261 yl (k(cat)/K(m) 3.9 +/- 0.5 m(-1) s(-1)), or methylmalonyl derivatives.

262 By substituting the natural methylmalonyl extender unit with a malonyl group, a mode

263 A, but by decarboxylation of an enzyme-bound methylmalonyl extender unit.

264 Malonyl and methylmalonyl extender units were found to be equivalent

265 rapamycin biosynthesis uses only malonyl and methylmalonyl extender units.

266 derive primer units via decarboxylation of a methylmalonyl extender.

267 ransferase (AT) domain of EpoC transfers the methylmalonyl moiety from methylmalonyl-CoA to the holo

268 ltransferase (AT) domain which transfers the methylmalonyl moiety of methylmalonyl-CoA onto the phosp

269 generated by decarboxylation of a malonyl or methylmalonyl moiety; normally, the decarboxylation step

270 the activity of the methylcitrate cycle, the methylmalonyl pathway, or incorporation of the propionyl

271 thase (KS) domain of EpoC decarboxylates the methylmalonyl-S-EpoC acyl enzyme to generate the carbon

272 a decarboxylative condensation with a paired methylmalonyl-SACP.

273 have been generated by replacing individual methylmalonyl-specific acyl transferase (AT) domains of

274 ephospho-CoA and its succinyl-, acetyl-, and methylmalonyl-thioester derivatives.

275 such attenuated mutant of DEBS, in which the methylmalonyl transferase domain of module 2 was replace

276 les containing either malonyl transferase or methylmalonyl transferase domains revealed a 15-20-fold

277 of amino acids between selected malonyl and methylmalonyl transferases, and found that a short (23-3