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1 phenicol acetyltransferase and dihydrolipoyl transacetylase.
2 ependent acetylation catalyzed by homoserine transacetylase.
3 solubilized and purified this PAF-dependent transacetylase 13,700-fold from rat kidney membranes (mi
5 stent with the notion that ATP regulates the transacetylase activity by reversible activation and ina
7 atase reduces the increased PAF:acyllyso-GPC transacetylase activity from the homogenates of ATP-acti
10 ed as PAF:lysoplasmalogen (lysophospholipid) transacetylase and PAF:sphingosine transacetylase, respe
11 C2-ceramide is produced via PAF:sphingosine transacetylase, and physiological levels of C2-ceramide
13 present study, we demonstrate that a similar transacetylase can transfer the acetate group from PAF t
14 ramphenicol acetyltransferase, dihydrolipoyl transacetylase, carnitine acetyltransferase, and VibH, a
15 cetyl-CoA only occurred upon addition of the transacetylase-catalyzing (lipoyl domain-free) inner cor
17 s a stronger response to the addition of the transacetylase component along with a better binding to
18 ffect is due largely to the inability of the transacetylase component of PDC to promote the phosphory
19 acetylation of the E. coli dihydrolipoamide transacetylase component, whereas crystallographic resul
23 ation induced by mitochondrial dihydrolipoyl transacetylase (DLAT), independent of the pyruvate dehyd
24 s, we identify upregulation of dihydrolipoyl transacetylase (DLAT), the E2-subunit of pyruvate dehydr
26 e dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase c
28 inner lipoyl domains (L2) from the 60-meric transacetylase (E2p) core of PDC, with concomitant stimu
29 pyruvate dehydrogenase (E1p), dihydrolipoyl transacetylase (E2p), and dihydrolipoamide dehydrogenase
35 e transsuccinylase (HTS, metA) or homoserine transacetylase (HTA; met2) for the biosynthesis of methi
36 reviously identified a novel CoA-independent transacetylase in the membrane fraction of HL-60 cells t
38 These results suggest that PAF-dependent transacetylase is an enzyme that modifies the cellular f
39 er lipoyl-bearing domain of dihydrolipoamide transacetylase (L2) determined with or without bound ade
42 r data show that both acetyltransferases and transacetylase participate in and contribute to the bios
43 nd that the CoA-independent PAF:acyllyso-GPC transacetylase recently identified by us is concurrently
47 ingosine, the CoA-independent, PAF-dependent transacetylase serves as a modifier of PAF, and sphingos
49 the acetyltransferases precedes that of the transacetylase with peak activation occurring at 1-2 min