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1 larly important to the catalytic activity of enoyl-CoA hydratase.
2 Glu139 are required for the high kcat of the enoyl-CoA hydratase.
3 i was identified as the catalytic residue of enoyl-CoA hydratase.
4 A ligase, and RpfF shows some relatedness to enoyl CoA hydratases.
5 ., E269 in aldehyde dehydrogenase-1; D204 in enoyl CoA hydratase-1), as well as residues of unknown f
6 thors show that exceeding nutrients suppress Enoyl-CoA hydratase-1 (ECHS1) activity by inducing its a
11 hat may contribute to renal function include enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase (EHH
12 l 3-oxoacyl-CoA thiolase (THIO), peroxisomal enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase (HD)
13 hree enzymes: fatty acyl-CoA oxidase (ACOX), enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase (HD)
15 lutaryl-CoA dehydrogenase also has intrinsic enoyl-CoA hydratase activity, a property of other member
16 ectra have been obtained for HD-CoA bound to enoyl-CoA hydratase, an enzyme system that has also prev
17 y and show another stable complex, PaaFG, an enoyl-CoA hydratase and enoyl-Coa isomerase, both belong
18 hexadienoyl-CoA (HD-CoA), bound to wild-type enoyl-CoA hydratase and G141P, a mutant in which a hydro
19 tyl-CoA when bound as an enolate to MCAD and enoyl-CoA hydratase and is used to rationalize the obser
20 ur separate reactions, two of which (2-trans enoyl-CoA hydratase and L-3-hydroxyacyl-CoA dehydrogenas
21 o contains the active site of long-chain 2,3-enoyl-CoA hydratase and long-chain 3-ketoacyl-CoA thiola
22 lytic properties of 3-ketoacyl-CoA thiolase, enoyl-CoA hydratase, and delta 3-cis-delta 2-trans-enoyl
25 th members of the crotonase family including enoyl-CoA hydratase (crotonase) and methylmalonyl-CoA de
27 Gene deletion analyses confirmed that the enoyl-CoA hydratase/dehydrogenase Fox2p, the putative 3-
28 termined the crystal structure of the enzyme enoyl-CoA hydratase (ECH) from rat liver with the bound
30 TFTH-CoA can be directly bioactivated by the enoyl-CoA hydratase (ECH) with the release of 1,2-dichlo
31 ium (PDB ID 3q1t) has been reported to be an enoyl-CoA hydratase (ECH), but SALSA analysis shows a po
33 ditions for crystallization of two proteins, enoyl-CoA hydratase from Mycobacterium tuberculosis and
34 ditions for crystallization of two proteins, enoyl-CoA hydratase from Mycobacterium tuberculosis and
35 noyl-coenzyme A (HD-CoA) bound to the enzyme enoyl-CoA hydratase has been determined using transferre
36 sidues (E164 and E144) in the active site of enoyl-CoA hydratase has been probed by site-directed mut
37 e promoter of the PPARalpha target genes rat enoyl-CoA hydratase (HD) and peroxisomal fatty acyl-CoA
40 athways associated with the members of the 2-enoyl-CoA hydratase/isomerase enzyme superfamily are com
41 esis, the active site of one member of the 2-enoyl-CoA hydratase/isomerase family, 4-chlorobenzoyl-Co
43 oxidation at the level of the second enzyme, enoyl-CoA hydratase/L-3-hydroxyacyl-CoA dehydrogenase (L
45 ex enhanced transcription from a peroxisomal enoyl-CoA hydratase/l-3-hydroxyacyl-CoA dehydrogenase bi
46 especially of CBP and TRAP150, to the mouse enoyl-CoA hydratase/l-3-hydroxyacyl-CoA dehydrogenase ge
47 urated substrates bind to the active site of enoyl-CoA hydratase, large spectral changes can be obser
48 of the component enzymes of TOC, long-chain enoyl-CoA hydratase, long-chain 3-hydroxyacyl-CoA dehydr
49 somal beta-oxidation mutants showed that the enoyl CoA-hydratase MAOC-1 serves an important role in a
51 eding experiments show that the MFP2 2-trans enoyl-CoA hydratase only exhibits activity against long
53 n genes trxA (Rv1470), trxB (Rv1471), and an enoyl-coA hydratase (Rv1472), indicating a possible role
54 ed enzymes, the acyl-CoA ligase SidI and the enoyl-CoA hydratase SidH, linking biosynthesis of mevalo
55 uence homology validates the modeling of the enoyl-CoA hydratase structure with the 4-(chlorobenzoyl)
56 G141 is part of a consensus sequence in the enoyl-CoA hydratase superfamily, the results presented h
58 coupled with the strong sequence homology to enoyl-CoA hydratase support the intramolecular suprafaci
59 wo conserved glutamate residues of rat liver enoyl-CoA hydratase to which Glu119 and Glu139 of the la
61 -fold decrease, respectively, in the kcat of enoyl-CoA hydratase without a significant change in the
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