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Literature summary for 1.1.1.37 extracted from

  • Maeda, T.; Koch-Koerfges, A.; Bott, M.
    Relevance of NADH dehydrogenase and alternative two-enzyme systems for growth of Corynebacterium glutamicum with glucose, lactate, and acetate (2020), Front. Bioeng. Biotechnol., 8, 621213 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.37

Cloned(Commentary)

Cloned (Comment) Organism
gene mdh, recombinant expression of MDH in differently engineered Corynebacterium glutamicum strains Corynebacterium glutamicum

Protein Variants

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/ Products (Substrates)

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

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 and Products (Substrate)

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

Synonyms Comment Organism
MDH
-
 Corynebacterium glutamicum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Corynebacterium glutamicum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Corynebacterium glutamicum

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Corynebacterium glutamicum
NADH
-
 Corynebacterium glutamicum

General Information

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