Cloned (Comment) | Organism |
---|---|
gene mdh, recombinant expression of MDH in differently engineered Corynebacterium glutamicum strains | Corynebacterium glutamicum |
Protein Variants | Comment | Organism |
---|---|---|
additional information | characterization of defined mutants lacking the non-proton-pumping NADH dehydrogenase Ndh (DELTAndh) and/or one of the alternative NADH-oxidizing enzymes, L-lactate dehydrogenase LdhA (DELTAldhA) and malate dehydrogenase Mdh (DELTAmdh). Together with the menaquinone-dependent L-lactate dehydrogenase LldD and malate:quinone oxidoreductase Mqo, the LdhA-LldD and Mdh-Mqo couples can functionally replace Ndh activity. In glucose minimal medium the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio, in line with Ndh being the major enzyme for NADH oxidation. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant, supporting an active role of the alternative Mdh-Mqo and LdhA-LldD systems in NADH oxidation and menaquinone reduction. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type, probably due to a higher activity of the menaquinone-dependent L-lactate dehydrogenase LldD. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR, suggesting that ldhA repression by the transcriptional regulator SugR prevented growth on L-lactate medium. Attempts to construct a DELTAndh/DELTAmdh/DELTAldhA triple mutant are not successful, suggesting that Ndh, Mdh and LdhA cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum | Corynebacterium glutamicum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-malate + NAD+ | Corynebacterium glutamicum | - |
oxaloacetate + NADH + H+ | - |
r | |
(S)-malate + NAD+ | Corynebacterium glutamicum ATCC 13032 | - |
oxaloacetate + NADH + H+ | - |
r | |
oxaloacetate + NADH + H+ | Corynebacterium glutamicum | - |
(S)-malate + NAD+ | - |
r | |
oxaloacetate + NADH + H+ | Corynebacterium glutamicum | - |
L-malate + NAD+ | - |
ir | |
oxaloacetate + NADH + H+ | Corynebacterium glutamicum LMG 3730 | - |
L-malate + NAD+ | - |
ir | |
oxaloacetate + NADH + H+ | Corynebacterium glutamicum BCRC 11384 | - |
L-malate + NAD+ | - |
ir | |
oxaloacetate + NADH + H+ | Corynebacterium glutamicum ATCC 13032 | - |
(S)-malate + NAD+ | - |
r | |
oxaloacetate + NADH + H+ | Corynebacterium glutamicum ATCC 13032 | - |
L-malate + NAD+ | - |
ir | |
oxaloacetate + NADH + H+ | Corynebacterium glutamicum JCM 1318 | - |
L-malate + NAD+ | - |
ir | |
oxaloacetate + NADH + H+ | Corynebacterium glutamicum NCIMB 10025 | - |
L-malate + NAD+ | - |
ir | |
oxaloacetate + NADH + H+ | Corynebacterium glutamicum DSM 20300 | - |
L-malate + NAD+ | - |
ir |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Corynebacterium glutamicum | - |
- |
- |
Corynebacterium glutamicum | Q8NN33 | - |
- |
Corynebacterium glutamicum ATCC 13032 | - |
- |
- |
Corynebacterium glutamicum ATCC 13032 | Q8NN33 | - |
- |
Corynebacterium glutamicum BCRC 11384 | Q8NN33 | - |
- |
Corynebacterium glutamicum DSM 20300 | Q8NN33 | - |
- |
Corynebacterium glutamicum JCM 1318 | Q8NN33 | - |
- |
Corynebacterium glutamicum LMG 3730 | Q8NN33 | - |
- |
Corynebacterium glutamicum NCIMB 10025 | Q8NN33 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-malate + NAD+ | - |
Corynebacterium glutamicum | oxaloacetate + NADH + H+ | - |
r | |
(S)-malate + NAD+ | - |
Corynebacterium glutamicum ATCC 13032 | oxaloacetate + NADH + H+ | - |
r | |
additional information | determination of intracellular NAD+/NADH ratios | Corynebacterium glutamicum | ? | - |
- |
|
additional information | determination of intracellular NAD+/NADH ratios | Corynebacterium glutamicum LMG 3730 | ? | - |
- |
|
additional information | determination of intracellular NAD+/NADH ratios | Corynebacterium glutamicum BCRC 11384 | ? | - |
- |
|
additional information | determination of intracellular NAD+/NADH ratios | Corynebacterium glutamicum ATCC 13032 | ? | - |
- |
|
additional information | determination of intracellular NAD+/NADH ratios | Corynebacterium glutamicum JCM 1318 | ? | - |
- |
|
additional information | determination of intracellular NAD+/NADH ratios | Corynebacterium glutamicum NCIMB 10025 | ? | - |
- |
|
additional information | determination of intracellular NAD+/NADH ratios | Corynebacterium glutamicum DSM 20300 | ? | - |
- |
|
oxaloacetate + NADH + H+ | - |
Corynebacterium glutamicum | (S)-malate + NAD+ | - |
r | |
oxaloacetate + NADH + H+ | - |
Corynebacterium glutamicum ATCC 13032 | (S)-malate + NAD+ | - |
r | |
oxaloacetate + NADH + H+ | - |
Corynebacterium glutamicum | L-malate + NAD+ | - |
ir | |
oxaloacetate + NADH + H+ | - |
Corynebacterium glutamicum LMG 3730 | L-malate + NAD+ | - |
ir | |
oxaloacetate + NADH + H+ | - |
Corynebacterium glutamicum BCRC 11384 | L-malate + NAD+ | - |
ir | |
oxaloacetate + NADH + H+ | - |
Corynebacterium glutamicum ATCC 13032 | L-malate + NAD+ | - |
ir | |
oxaloacetate + NADH + H+ | - |
Corynebacterium glutamicum JCM 1318 | L-malate + NAD+ | - |
ir | |
oxaloacetate + NADH + H+ | - |
Corynebacterium glutamicum NCIMB 10025 | L-malate + NAD+ | - |
ir | |
oxaloacetate + NADH + H+ | - |
Corynebacterium glutamicum DSM 20300 | L-malate + NAD+ | - |
ir |
Synonyms | Comment | Organism |
---|---|---|
MDH | - |
Corynebacterium glutamicum |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Corynebacterium glutamicum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Corynebacterium glutamicum |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Corynebacterium glutamicum | |
NADH | - |
Corynebacterium glutamicum |
General Information | Comment | Organism |
---|---|---|
malfunction | in glucose minimal medium, the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR. Ndh, Mdh and LdhA together cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum | Corynebacterium glutamicum |
metabolism | the oxidation of NADH with the concomitant reduction of a quinone is a crucial step in the metabolism of respiring cells. Relevance of three different NADH oxidation systems in the actinobacterial model organism Corynebacterium glutamicum: non-proton-pumping NADH dehydrogenase (Ndh), and NADH-oxidizing enzymes, L-lactate dehydrogenase (LdhA) and malate dehydrogenase (Mdh) | Corynebacterium glutamicum |
physiological function | the enzyme is required for oxidation of NADH. The net reaction of the Mdh-Mqo couple equals that of an Ndh and it can serve as an alternative NADH dehydrogenase, as Mdh reduces oxaloacetate with NADH to L-malate, and the membrane-associated malate:quinone oxidoreductase (Mqo) subsequently re-oxidizes L-malate back to oxaloacetate and reduces menaquinone (MK) | Corynebacterium glutamicum |