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Results 1 - 10 of 13 > >>
EC Number General Information Commentary Reference
Show all pathways known for 1.1.2.3Display the word mapDisplay the reaction diagram Show all sequences 1.1.2.3evolution the catalytic domains of GOX3 and CYB2, the yeast L-lactate cytochrome c oxidoreductase, are homologous (40% identity and 57% similarity) 743494
Show all pathways known for 1.1.2.3Display the word mapDisplay the reaction diagram Show all sequences 1.1.2.3malfunction the growth of the disruptant of cyb2A encoding a cytochrome b2 lactate dehydrogenase in Pichia kudriavzevii is severely impaired on medium supplemented with L-lactate -, 763149
Show all pathways known for 1.1.2.3Display the word mapDisplay the reaction diagram Show all sequences 1.1.2.3metabolism Cyb2Ap plays a crucial role in the use of L-lactate -, 763149
Show all pathways known for 1.1.2.3Display the word mapDisplay the reaction diagram Show all sequences 1.1.2.3metabolism the pyruvate produced as a result of L-lactate oxidation is utilised by the Krebs cycle, but flavocytochrome b2 also forms part of a short respiratory electron transport chain which results in one ATP molecule being produced for every L-lactate consumed 695890
Show all pathways known for 1.1.2.3Display the word mapDisplay the reaction diagram Show all sequences 1.1.2.3more molecular dynamics simulations using a hybrid quantum mechanics/molecular mechanics (QM/MM) scheme to study the mechanism of L-lactate oxidation by flavocytochrome b2. Simulation results highlight the influence of the environment on the catalytic mechanism by describing a step-wise process in the wild-type enzyme with R289 in a distal position and a concerted mechanism for the other systems. Structure analysis of pyruvate in the Fcb2 active site pocket with R289 in the distal conformation. Residue Y254 plays a role in the catalytic process by stabilizing the product of the first proton transfer from substrate to H373, while residue D282 is expected to stabilize the imidazolium ion in transition and product states by electrostatic interactions and hydrogen bonding with the Hdelta of H373. Active site structures of wild-type and mutant enzymes, detailed overview 743420
Show all pathways known for 1.1.2.3Display the word mapDisplay the reaction diagram Show all sequences 1.1.2.3more of the three glycolate oxidases in Arabidopsis thaliana, only GOX3 can efficiently metabolize L-lactate at low intracellular concentrations 743494
Show all pathways known for 1.1.2.3Display the word mapDisplay the reaction diagram Show all sequences 1.1.2.3physiological function disruption of the lldD gene impairs the growth of this strain in L-lactate, but the mutant strain is still able to grow after a long lag phase. Deletion of both the LldD and LldA genes completely impairs the L-lactate utilization capacity of the strain 760998
Show all pathways known for 1.1.2.3Display the word mapDisplay the reaction diagram Show all sequences 1.1.2.3physiological function flavocytochrome b2, i.e. L-lactate cytochrome c oxidoreductase, catalyzes L-lactate oxidation at the expense of cytochrome c and enables the latter to grow on lactate as the sole carbon source 696302
Show all pathways known for 1.1.2.3Display the word mapDisplay the reaction diagram Show all sequences 1.1.2.3physiological function glycolate oxidase3, a glycolate oxidase homolog of yeast L-lactate cytochrome c oxidoreductase, supports L-lactate oxidation in roots of Arabidopsis thaliana 743494
Show all pathways known for 1.1.2.3Display the word mapDisplay the reaction diagram Show all sequences 1.1.2.3physiological function in roots of Arabidopsis thaliana, L-lactate is generated by the reduction of pyruvate via L-lactate dehydrogenase, EC 1.1.1.27, but this enzyme does not efficiently catalyze the reverse reaction. Glycolate oxidase GOX3 is the enzyme that metabolizes L-lactate to pyruvate in vivo and may ensure the sustainment of low levels of L-lactate after its formation under normoxia. GOX3 does not display activity with natural electron acceptors such as cytochrome c, NAD+, or NADP+ suggests that it does not act as dehydrogenases in vivo. GOX3 plays a more prominent role in heterotrophic tissue than in autotrophic tissues. Enzyme GOX3 can rescue the cyb2 lethal phenotype in Saccharomyces cerevisiae. Possible involvement of GOX3 in controlling L-lactate homeostasis in roots 743494
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