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1 ble to grow in the presence of oils, while a malate synthase (aceB) deletion mutant grew more slowly
2 Genes encoding isocitrate lyase (aceA) and malate synthase (aceB), both involved in the carbon cons
5 MclA1) that is assumed to be responsible for malate synthase activity still grows on C(2) compounds.
7 as an essential physiologic function of Mtb malate synthase and advances its validation as a target
10 ate cycle (GC) enzymes, isocitrate lyase and malate synthase, are expressed in a tissue- and stage-sp
12 ay should require glyoxylate consumption via malate synthase, but a mutant lacking malyl-CoA/beta-met
14 pecifically isocitrate lyase (DeltaaceA) and malate synthase (DeltaaceB), suggested that the complete
15 yoxylate cycle, isocitrate lyase (TaICL) and malate synthase, diverged in their expression between su
16 tudy the genes encoding isocitrate lyase and malate synthase from Chlorogloeopsis fritschii PCC 9212
17 y to gene sequences for isocitrate lyase and malate synthase from plants and other fungal species.
18 logy to 3D NOESY spectra of Escherichia coli Malate Synthase G (81 kDa), where observed NOE cross-pea
20 in {U-(2)H; Ala(beta)-[(13)CHD(2)]}-labeled Malate Synthase G (MSG)--an 82-kDa monomeric enzyme that
21 Leu,Val-[13CH3/12CD3]}-labeled 82-kDa enzyme Malate Synthase G and is expected to accelerate NMR-base
22 de response regulator (soxR), the gene for a malate synthase G homologue (glcG), an antisense transcr
23 al structure of selenomethionine-substituted malate synthase G, an 81 kDa monomeric enzyme from Esche
25 lic acid cycle in which isocitrate lyase and malate synthase (GlcB) catalyze the net incorporation of
26 We have used a fragment-based approach on malate synthase (GlcB) from Mycobacterium tuberculosis a
27 anscript abundances for isocitrate lyase and malate synthase increased, and C. fritschii grew faster,
28 gh experiments the involvement of vertebrate malate synthase-like genes in the conversion of (S)-urei
29 ate cycle enzymes isocitrate lyase (ICL) and malate synthase (MLS) are replaced by photorespiration e
32 hese studies provide evidence that the M. tb malate synthase (MS) has adapted to function as an adhes
33 a carbon source, isocitrate lyase (ICL) and malate synthase (MS) mRNAs increase significantly in amo
36 both chimeric leaders and one from isopropyl malate synthase that possesses a negative charge that th
37 orted the activities of isocitrate lyase and malate synthase, the key enzymes of the glyoxylate cycle
38 irst 11 residues were deleted from isopropyl malate synthase, the resulting protein was imported more
39 n metabolism, specifically isocitrate lyase, malate synthase, transaldolase, fructose bisphosphatase
40 glyoxylate shunt genes (isocitrate lyase and malate synthase) was >300-fold higher in the light--but
41 lcB gene from M. tuberculosis, which encodes malate synthase, was cloned, and GlcB was expressed in E
42 When the genes encoding isocitrate lyase and malate synthase were expressed in Synechococcus sp. PCC
43 yoxylate cycle this reaction is catalyzed by malate synthase, whereas in the ethylmalonyl-CoA pathway
44 recognition are discussed in comparisons of malate synthase with pyruvate kinase and pyruvate phosph