Results 161 to 170 of about 57,138 (236)
Mohangic Acid H and Mohangiol: New <i>p</i>-Aminoacetophenone Derivatives from a Mudflat-Derived <i>Streptomyces</i> sp. [PDF]
Son J, Lee JH, Cho YJ, Moon K, Bae M.
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Comparative Proteomic Analysis of <i>Acremonium chrysogenum</i> Strains: Key Changes Converting the Wild-Type Strain into Antibiotic Cephalosporin C Biofactory. [PDF]
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Apparent isocitrate lyase activity in Leishmania amazonensis
Acta Parasitologica, 2017AbstractEarly reports have demonstrated the occurrence of glyoxylate cycle enzymes in ...
Concepción, Hernández-Chinea +4 more
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Advances in Mycobacterial Isocitrate Lyase Targeting and Inhibitors
Current Medicinal Chemistry, 2012Isocitrate lyase plays a key role for survival of Mycobacterium tuberculosis in the latent form during a chronic stage of infection. This enzyme is important for M. tuberculosis during steady stage growth when it converts isocitrate to succinate and glyoxylate. Then, the glyoxylate is condensed with acetyl-CoA to form malate by malate synthase.
M, Krátký, J, Vinšová
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Phosphorylation of acinetobacter isocitrate lyase
Biochemical and Biophysical Research Communications, 1992During growth on succinate, Acinetobacter calcoaceticus contains two forms of the enzyme isocitrate dehydrogenase. Addition of acetate to a lag-phase culture grown on succinate causes a dramatic increase in activity of form II of isocitrate dehydrogenase and in isocitrate lyase.
J C, Hoyt, H C, Reeves
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Isocitrate lyase from higher plants
Phytochemistry, 1987Abstract Work on isocitrate lyase, the first enzyme unique to the glyoxylate cycle, is reviewed.
GIACHETTI, EUGENIO +4 more
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Isocitrate lyase of conifers (Pinus pinea
International Journal of Biochemistry, 19821. Isocitrate lyase has been purified about 60 times from the conifer Pinus pinea. A first characterization was made. 2. The high instability is an important feature of this enzyme from higher plants, this causes serious problems in the purification and characterization. 3.
PINZAUTI, GIANCARLO +2 more
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Active site modification of isocitrate lyase
Biochemical and Biophysical Research Communications, 1969Abstract β-Bromopyruvate (BrP) alkylates isocitrate lyase at the active site as indicated by the following: (1) the irreversible alkylation shows saturation kinetics, (2) substrate, isocitrate, is a competitive inhibitor of inactivation by BrP, (3) the combination of products, glyoxylate and succinate, or a competitive inhibitor of the enzyme ...
T E, Roche, B A, McFadden
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