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Literature summary for 1.1.1.67 extracted from
- Modular simulation to determine the optimal operating policy of a batch reactor for the enzymatic fructose reduction to mannitol with the in situ continuous enzymatic regeneration of the NAD cofactor (2017), Rev. Chim., 68, 2196-2203 .
No PubMed abstract available
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | mannitol is a natural hexitol with important applications in medicine and food industry. Development of a production method on an industrial scale, optimization and evaluation of production in a batch reactor (BR, or BRP operation) for a complex bi-enzymatic system with suspended enzymes and cofactor regeneration, method modeling, molecular calculations and simulations, detailed overview | Pseudomonas fluorescens |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene mtlD, recombinant overexpression of the enzyme in Escherichia coli strain JM109 | Pseudomonas fluorescens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | application of a modular screening procedure that can identify the optimal operating policy of an enzymatic reactor, which minimizes the enzyme consumption, given the process kinetic model, and an imposed production capacity. Following an optimization procedure, the process effectiveness is evaluated in a systematic approach, by including simple batch reactor (BR), batch with intermittent addition of the key-enzyme following certain optimal policies (BRP). The enzymatic reduction of D-fructose to mannitol is used as a model system utilizing suspended MDH (mannitol dehydrogenase) and NADH (nicotinamide adenine dinucleotide) cofactor, with the in-situ continuous regeneration of the cofactor by the expense of formate degradation in the presence of suspended FDH (formate dehydrogenase). The NADH-dependent FDH and MDH typical activity in D-fructose reduction is of 1-2 U/ml in a batch reactor | Pseudomonas fluorescens |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetic modeling | Pseudomonas fluorescens |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-fructose + NADH + H+ | Pseudomonas fluorescens | - |
D-mannitol + NAD+ | - |
r |  |
| D-fructose + NADH + H+ | Pseudomonas fluorescens DSM 50106 | - |
D-mannitol + NAD+ | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas fluorescens | O08355 | - |
- |
| Pseudomonas fluorescens DSM 50106 | O08355 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme from Escherichia coli strain JM109 | Pseudomonas fluorescens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-fructose + NADH + H+ | - |
Pseudomonas fluorescens | D-mannitol + NAD+ | - |
r | |
| D-fructose + NADH + H+ | - |
Pseudomonas fluorescens DSM 50106 | D-mannitol + NAD+ | - |
r | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| mannitol dehydrogenase | - |
Pseudomonas fluorescens |
| MDH | - |
Pseudomonas fluorescens |
| MtlD | - |
Pseudomonas fluorescens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Pseudomonas fluorescens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Pseudomonas fluorescens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | - |
Pseudomonas fluorescens | |
| NADH | - |
Pseudomonas fluorescens | |
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