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Literature summary for 4.1.2.25 extracted from
- One substrate, five products: reactions catalyzed by the dihydroneopterin aldolase from Mycobacterium tuberculosis (2012), J. Am. Chem. Soc., 134, 19758-19771.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.00016 | - |
7,8-dihydroneopterin | pH 7.0, 22°C | Mycobacterium tuberculosis |  |
| 0.00017 | - |
7,8-dihydromonapterin | pH 7.0, 22°C | Mycobacterium tuberculosis | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | no metal required | Mycobacterium tuberculosis |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 16585 | - |
apo-enzyme, 4 * 16585, and octamer for 7,8-dihydroxanthopterin-bound form, 8 * 16585, mass spectrometry | Mycobacterium tuberculosis |
| 62300 | - |
apo-enzyme, mass spectrometry | Mycobacterium tuberculosis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycobacterium tuberculosis | P9WNC5 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde | - |
Mycobacterium tuberculosis | 7,8-dihydroneopterin + 7,8-dihydromonapterin | reaction is reversible, and C-C bond formation has both 7,8-dihydroneopterin and 7,8-dihydromonapterin as products plus 7,8-dihydroxanthopterin | r | |
| 7,8-dihydromonapterin | - |
Mycobacterium tuberculosis | 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde | - |
r | |
| 7,8-dihydroneopterin | - |
Mycobacterium tuberculosis | 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde | - |
r | |
| additional information | enzyme can utilize both dihydroneopterin and 7,8-dihydromonapterin as substrates to generate 6-hydroxymethyl-7,8-dihydropterin. The reaction generates three different pterin products, one of which is not produced by other wild-type dihydroneopterin aldolases. The enzyme-substrate complex partitions 51% in the first turnover to form the aldolase products, 24% to the epimerase product and 25% to the oxygenase products. The aldolase reaction is strongly pH dependent. Chemistry is rate limiting for the aldolase reaction, and two protons and a likely solvent contribution are involved in formation and breakage of a common intermediate | Mycobacterium tuberculosis | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| tetramer | apo-enzyme, 4 * 16585, and octamer for 7,8-dihydroxanthopterin-bound form, 8 * 16585, mass spectrometry | Mycobacterium tuberculosis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DHNA | - |
Mycobacterium tuberculosis |
| FolB | - |
Mycobacterium tuberculosis |
| Rv3607c | - |
Mycobacterium tuberculosis |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0054 | - |
7,8-dihydroneopterin | pH 7.0, 22°C | Mycobacterium tuberculosis | |
| 0.006 | - |
7,8-dihydromonapterin | pH 7.0, 22°C | Mycobacterium tuberculosis | |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 36 | - |
7,8-dihydroneopterin | pH 7.0, 22°C | Mycobacterium tuberculosis | |
| 38 | - |
7,8-dihydromonapterin | pH 7.0, 22°C | Mycobacterium tuberculosis | |
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