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

20 the vitamin B12 (cobalamin)-dependent enzyme 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 log of the natural ACP-bound substrate, with methylmalonyl-CoA (MM-CoA) in the absence of NADPH gave

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

65 0-kDa protein inhibited the incorporation of methylmalonyl-CoA into fatty acids by SMAS.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

105 Methylmalonyl-CoA mutase belongs to the class of adenosy

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

107 Methylmalonyl-CoA mutase catalyzes the adenosylcobalamin

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

109 Methylmalonyl-CoA mutase catalyzes the isomerization of

110 Methylmalonyl-CoA mutase catalyzes the isomerization of

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

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

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

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

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

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

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

118 Methylmalonyl-CoA mutase is a key enzyme in intermediary

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

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

121 Methylmalonyl-CoA mutase is an adenosylcobalamin (AdoCbl

122 Methylmalonyl-CoA mutase is an adenosylcobalamin-depende

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

140 2-dependent enzymes, methionine synthase and methylmalonyl-CoA mutase.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

156 Because methylmalonyl-CoA mutases are involved in the metabolism

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

207 2S,3R)-2-methyl-3-hydroxypentanoyl-SNAC (5), methylmalonyl-CoA, and NADPH with the recombinant [KS6][

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

236 Malonyl and methylmalonyl extender units were found to be equivalent

237 rapamycin biosynthesis uses only malonyl and methylmalonyl extender units.

238 derive primer units via decarboxylation of a methylmalonyl extender.

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

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

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

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

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

244 a decarboxylative condensation with a paired methylmalonyl-SACP.

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

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

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

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

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