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Literature summary for 1.1.1.361 extracted from
- Carbocyclic substrate analogues reveal kanosamine biosynthesis begins with the alpha-anomer of glucose 6-phosphate (2020), ACS Chem. Biol., 15, 2205-2211 .
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| NADH | product inhibition | Bacillus subtilis |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | steady-state kinetics. Kinetics of NtdC by itself and with the next enzyme in the pathway, NtdA, which converts 3-oxo-D-glucose 6-phosphate to kanosamine 6-phosphate through a glutamate-coupled PLP-dependent transamination, have shown that the equilibrium of both the NtdC reaction and the NtdC-NtdA-coupled reaction lies heavily toward D-glucose 6-phosphate | Bacillus subtilis | |
| 0.48 | - |
NAD+ | pH 9.5, 25°C, recombinant enzyme NtdC | Bacillus subtilis | |
| 1.9 | - |
D-glucose 6-phosphate | pH 9.5, 25°C, recombinant enzyme NtdC | Bacillus subtilis | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-glucose 6-phosphate + NAD+ | Bacillus subtilis | - |
3-dehydro-D-glucose 6-phosphate + NADH + H+ | - |
? | |
| D-glucose 6-phosphate + NAD+ | Bacillus subtilis 168 | - |
3-dehydro-D-glucose 6-phosphate + NADH + H+ | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | O07564 | - |
- |
| Bacillus subtilis 168 | O07564 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| carbaglucose 6-phosphate + NAD+ | - |
Bacillus subtilis | ? + NADH + H+ | - |
? | |
| carbaglucose 6-phosphate + NAD+ | - |
Bacillus subtilis 168 | ? + NADH + H+ | - |
? | |
| D-glucose 6-phosphate + NAD+ | - |
Bacillus subtilis | 3-dehydro-D-glucose 6-phosphate + NADH + H+ | - |
? | |
| D-glucose 6-phosphate + NAD+ | the alpha-anomer form is the substrate for the enzyme. Kinetics of NtdC by itself and with the next enzyme in the pathway, NtdA, which converts 3-oxo-D-glucose 6-phosphate to kanosamine 6-phosphate through a glutamate-coupled PLP-dependent transamination, have shown that the equilibrium of both the NtdC reaction and the NtdC-NtdA-coupled reaction lies heavily toward D-glucose 6-phosphate | Bacillus subtilis | 3-dehydro-D-glucose 6-phosphate + NADH + H+ | - |
? | |
| D-glucose 6-phosphate + NAD+ | - |
Bacillus subtilis 168 | 3-dehydro-D-glucose 6-phosphate + NADH + H+ | - |
? | |
| D-glucose 6-phosphate + NAD+ | the alpha-anomer form is the substrate for the enzyme. Kinetics of NtdC by itself and with the next enzyme in the pathway, NtdA, which converts 3-oxo-D-glucose 6-phosphate to kanosamine 6-phosphate through a glutamate-coupled PLP-dependent transamination, have shown that the equilibrium of both the NtdC reaction and the NtdC-NtdA-coupled reaction lies heavily toward D-glucose 6-phosphate | Bacillus subtilis 168 | 3-dehydro-D-glucose 6-phosphate + NADH + H+ | - |
? | |
| additional information | the NtdC-catalyzed reaction is unusual because 3-oxo-D-glucose 6-phosphate undergoes rapid ring opening, resulting in a 1,3-dicarbonyl compound that is inherently unstable due to enolate formation. Synthesis of carbocyclic G6P analogues by two routes, one based upon the Ferrier II rearrangement to generate the carbocycle and one based upon a Claisen rearrangement. Both pseudo-anomers of carbaglucose 6-phosphate (C6P) are synthesized using the Ferrier approach, and activity assays reveal that the pseudo-alpha-anomer is a good substrate for NtdC, while the pseudo-beta-anomer and the open-chain analogue, sorbitol 6-phosphate (S6P), are not substrates. A more efficient synthesis of alpha-C6P is achieved using the Claisen rearrangement approach, which allows for a thorough evaluation of the NtdC-catalyzed oxidation of alpah-C6P | Bacillus subtilis | ? | - |
- |
|
| additional information | the NtdC-catalyzed reaction is unusual because 3-oxo-D-glucose 6-phosphate undergoes rapid ring opening, resulting in a 1,3-dicarbonyl compound that is inherently unstable due to enolate formation. Synthesis of carbocyclic G6P analogues by two routes, one based upon the Ferrier II rearrangement to generate the carbocycle and one based upon a Claisen rearrangement. Both pseudo-anomers of carbaglucose 6-phosphate (C6P) are synthesized using the Ferrier approach, and activity assays reveal that the pseudo-alpha-anomer is a good substrate for NtdC, while the pseudo-beta-anomer and the open-chain analogue, sorbitol 6-phosphate (S6P), are not substrates. A more efficient synthesis of alpha-C6P is achieved using the Claisen rearrangement approach, which allows for a thorough evaluation of the NtdC-catalyzed oxidation of alpah-C6P | Bacillus subtilis 168 | ? | - |
- |
|
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| G6P 3-dehydrogenase | - |
Bacillus subtilis |
| ntdC | - |
Bacillus subtilis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Bacillus subtilis |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 2 | - |
NAD+ | pH 9.5, 25°C, recombinant enzyme NtdC | Bacillus subtilis | |
| 2 | - |
D-glucose 6-phosphate | pH 9.5, 25°C, recombinant enzyme NtdC | Bacillus subtilis | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 9.5 | - |
- |
Bacillus subtilis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | - |
Bacillus subtilis | |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.2 | - |
NADH | pH 9.5, 25°C, recombinant enzyme NtdC | Bacillus subtilis | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the requirement for the alpha-anomer as substrate indicates that NtdC and NtdA, the subsequent enzyme in the pathway, have co-evolved to recognize the alpha-anomer in order to avoid mutarotation between enzymatic steps | Bacillus subtilis |
| metabolism | NtdC is an NAD-dependent dehydrogenase that catalyzes the conversion of glucose 6-phosphate (G6P) to 3-oxoglucose 6-phosphate, the first step in kanosamine biosynthesis in Bacillus subtilis and other closely-related bacteria. Kanosamine biosynthesis in Bacillus subtilis, overview | Bacillus subtilis |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.05 | - |
D-glucose 6-phosphate | pH 9.5, 25°C, recombinant enzyme NtdC | Bacillus subtilis | |
| 4.17 | - |
NAD+ | pH 9.5, 25°C, recombinant enzyme NtdC | Bacillus subtilis | |
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