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evolution
two evolutionarily distinct families of LDH enzymes perform the oxidation of NADH/reduction of NAD+ to yield a product that differs only in its chirality: L-lactate or D-lactate
evolution
although both types of enzymes, NAD-dependent D- and L-lactate dehydrogenases (D-LDH, EC 1.1.1.28; and L-LDH, EC 1.1.1.27) catalyze identical reactions except for the distinct chirality of the lactate product, they are evolutionarily distinct from each other. Allosteric mechanism of D-LDHs, overview
evolution
although both types of enzymes, NAD-dependent D- and L-lactate dehydrogenases (D-LDH, EC 1.1.1.28; and L-LDH, EC 1.1.1.27) catalyze identical reactions except for the distinct chirality of the lactate product, they are evolutionarily distinct from each other. Allosteric mechanism of D-LDHs, overview
evolution
although both types of enzymes, NAD-dependent D- and L-lactate dehydrogenases (D-LDH, EC 1.1.1.28; and L-LDH, EC 1.1.1.27) catalyze identical reactions except for the distinct chirality of the lactate product, they are evolutionarily distinct from each other. Allosteric mechanism of D-LDHs, overview
evolution
the enzyme belongs to the D-isomer-specific 2-hydroxyacid dehydrogenase family
evolution
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the enzyme belongs to the D-isomer-specific 2-hydroxyacid dehydrogenase family
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evolution
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although both types of enzymes, NAD-dependent D- and L-lactate dehydrogenases (D-LDH, EC 1.1.1.28; and L-LDH, EC 1.1.1.27) catalyze identical reactions except for the distinct chirality of the lactate product, they are evolutionarily distinct from each other. Allosteric mechanism of D-LDHs, overview
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metabolism
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in the organism, xylose is converted into lactic and acetic acids by xylose isomerization by xylose isomerase to xylulose, which is phosphorylated to xylulose 5-phosphate by xylulokinase. Through the phosphoketolase pathway, xylulose 5-phosphate is finally converted to lactic acid and acetic acid in a process known as hetero-lactic acid fermentation
metabolism
the enzyme acts at the last step of the glycolytic pathway under anaerobic conditions
metabolism
the enzyme acts at the last step of the glycolytic pathway under anaerobic conditions
metabolism
the enzyme acts at the last step of the glycolytic pathway under anaerobic conditions
metabolism
amino acid residues I177 and N213 form a gate guarding the NAD adenine moiety binding cavity
metabolism
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in the organism, xylose is converted into lactic and acetic acids by xylose isomerization by xylose isomerase to xylulose, which is phosphorylated to xylulose 5-phosphate by xylulokinase. Through the phosphoketolase pathway, xylulose 5-phosphate is finally converted to lactic acid and acetic acid in a process known as hetero-lactic acid fermentation
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metabolism
Lactiplantibacillus plantarum NCIMB 8826 delta ldhL1 -xpk1::tkt-delta xpk
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in the organism, xylose is converted into lactic and acetic acids by xylose isomerization by xylose isomerase to xylulose, which is phosphorylated to xylulose 5-phosphate by xylulokinase. Through the phosphoketolase pathway, xylulose 5-phosphate is finally converted to lactic acid and acetic acid in a process known as hetero-lactic acid fermentation
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metabolism
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the enzyme acts at the last step of the glycolytic pathway under anaerobic conditions
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physiological function
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thermostable D-lactate dehydrogenase is a key enzyme for the production of the D-form of lactic acid from pyruvate concomitant with the oxidation of NADH to NAD+
physiological function
a deletion mutant lacking all four NADH dehydrogenases retains the ability to grow on N-acetylglucosamine under fumarate-respiring conditions, while an additional deletion of LdhA or respiratory quinone-dependent D-LDH deprives the mutant of this growth ability
physiological function
D-lactate is a key intermediate metabolite of the mobilization of lipids and glycogen. Deletion of D-lactate dehydrogenase DLD1 causes defects in conidiogenesis and appressorium formation, and subsequently the loss of fungal pathogenicity. DLD1 activity is involved in the maintenance of redox homeostasis during conidial germination
physiological function
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gene LdhR encoding an LysR-type transcriptional regulator is cotranscribed with D-lactate dehydrogenase gene LdhA. The overexpression of LdhA in a LdhR deletion mutant partially restores the reduced cell aggregate size and reduced surface-attached biofilms of the mutant
physiological function
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isoform D-LDH1 is the major enzyme responsible for D-lactic acid production in Leuconostoc mesenteroides J18
physiological function
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D-lactate is a key intermediate metabolite of the mobilization of lipids and glycogen. Deletion of D-lactate dehydrogenase DLD1 causes defects in conidiogenesis and appressorium formation, and subsequently the loss of fungal pathogenicity. DLD1 activity is involved in the maintenance of redox homeostasis during conidial germination
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physiological function
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isoform D-LDH1 is the major enzyme responsible for D-lactic acid production in Leuconostoc mesenteroides J18
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additional information
ldhD transcription levels are higher than those of ldhL, EC 1.1.1.27
additional information
ldhD transcription levels are higher than those of ldhL, EC 1.1.1.27
additional information
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ldhD transcription levels are higher than those of ldhL, EC 1.1.1.27
additional information
ldhL, EC 1.1.1.27, transcription levels are higher than those of ldhD
additional information
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ldhL, EC 1.1.1.27, transcription levels are higher than those of ldhD
additional information
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the side chain of residue Tyr52 locates very near the C3 substituent group of 2-ketoacid substrate and is associated with the recognition of substrate side chain
additional information
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ldhD transcription levels are higher than those of ldhL, EC 1.1.1.27
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additional information
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ldhD transcription levels are higher than those of ldhL, EC 1.1.1.27
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additional information
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ldhL, EC 1.1.1.27, transcription levels are higher than those of ldhD
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