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1 and Dh-FADH(-) that converts crotonyl-CoA to butyryl-CoA.
2 ansfers enable Bcd to reduce crotonyl-CoA to butyryl-CoA.
3 skeleton rearrangement of isobutyryl-CoA to butyryl-CoA.
4 h the priming of the enzyme by acetyl-CoA or butyryl-CoA.
5 ng acetyl-CoA approximately propionyl-CoA >> butyryl-CoA.
6 to Bcd for the reduction of crotonyl-CoA to butyryl-CoA.
7 ansfers enable Bcd to reduce crotonyl-CoA to butyryl-CoA.
8 n which is distinct from the metabolism of n-butyryl-CoA.
9 9-h lag in growth was observed, during which butyryl-CoA, a degradation product of ethylmalonyl-CoA,
11 ere analyzed for 16S rRNA sequencing and the butyryl-CoA:acetateCoA transferase (BCoAT) gene expressi
12 e, acetoacetyl coenzyme A (acetoacetyl-CoA), butyryl CoA, acetoacetate, and beta-hydroxybutyrate.
14 the interconversion of isobutyryl-CoA and n-butyryl-CoA also catalyzes the interconversion between i
16 nthesis in S. collinus, which suggested that butyryl-CoA and isobutyryl-CoA function as starter units
19 oA dehydrogenase has maximal activity toward butyryl-CoA and negligible activity toward substrates lo
23 tical to those seen for MM-CoA; in addition, butyryl-CoA binds and behaves in a manner similar to pro
24 e biosynthesis and that either acetyl-CoA or butyryl-CoA can be a starter unit for palmitate biosynth
25 ssigned to bcd(red):crotonyl-CoA and bcd(ox):butyryl-CoA charge-transfer complexes, demonstrating the
28 enzyme caused the midpoint potential for the butyryl-CoA/crotonyl-CoA couple (E(BCoA/CCoA)) to shift
30 dies, the biosynthesis of the palmitate from butyryl-CoA decreases in the presence of thiolactomycin.
31 and rapid-reaction kinetics of the isolated butyryl-CoA dehydrogenase (bcd) component of the electro
32 Electron-transferring flavoprotein (Etf) and butyryl-CoA dehydrogenase (Bcd) from Acidaminococcus fer
33 A (CoA) dehydrogenase (BHBD), crotonase, and butyryl-CoA dehydrogenase (BCD) from Clostridium acetobu
35 a-FADH(-)) transfers one electron further to butyryl-CoA dehydrogenase (Bcd); two such transfers enab
36 a-FADH(-)) transfers one electron further to butyryl-CoA dehydrogenase (Bcd); two such transfers enab
37 with alpha-FAD and beta-FAD) and tetrameric butyryl-CoA dehydrogenase (Bcd, with delta-FAD in each s
38 ectron transferring flavoprotein (EtfAf) and butyryl-CoA dehydrogenase (BcdAf) of Acidaminococcus fer
40 ween an acetyl-, propionyl-, isobutyryl-, or butyryl-CoA derived primer unit and a malonyl-CoA derive
41 M), which interconverts isobutyryl-CoA and n-butyryl-CoA; ethylmalonyl-CoA mutase, which interconvert
42 at CCR plays a significant role in providing butyryl-CoA for monensin A biosynthesis and is present i
43 reductase, which converts acetoacetyl-CoA to butyryl-CoA for use as a 4C extender unit during tylacto
45 yme A (CoA) derivatives, such as acetyl-CoA, butyryl-CoA, HMG-CoA, and malonyl-CoA, as well as NADPH
47 catalyzes the conversion of crotonyl-CoA to butyryl-CoA in the presence of NADPH, was previously clo
48 EBS 1+TE can convert acetyl-, propionyl-, or butyryl-CoA into the corresponding C8-, C9-, and C10-lac
50 talyze the condensation of malonyl-pfACP and butyryl-CoA (k(cat) 200 min(-1), K(M) 35.7 +/- 4.4 micro
51 substrate specificity and is able to accept butyryl-CoA, leading to the production of polyketides wi
52 bcd with crotonyl-CoA and oxidized bcd with butyryl-CoA, long-wavelength-absorbing intermediates are
53 he high concentration of 4-hydroxy-4-phospho-butyryl-CoA may be related to the cerebral dysfunction o
54 imple equation: crotonyl-CoA + NADH + H(+) = butyryl-CoA + NAD(+) with Km = 1.4 mum ferredoxin or 2.0
57 tase, a primary metabolic enzyme involved in butyryl-CoA production in streptomycetes, was expressed
64 e the exergonic reduction of crotonyl-CoA to butyryl-CoA to the endergonic reduction of ferredoxin bo
65 lmitate (a branched-chain fatty acid), while butyryl-CoA was converted to palmitate (a straight-chain
66 in 824(pAADB1) fermentations suggested that butyryl-CoA was limiting butanol production in 824(pAADB
70 f the loading didomain, although acetyl- and butyryl-CoA were also accepted with approximately 40-fol
71 the interconversion of isobutyryl-CoA and n-butyryl-CoA, whereas GTPase activity is associated with
72 ensation of two acetyl-CoA molecules to form butyryl-CoA, which is then transformed to succinyl-CoA w
75 action (lactate + crotonyl-CoA -> pyruvate + butyryl-CoA) yielded a k(cat) of 2.5 +/- 0.1 s(-1) and a