Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | impact of alpha-subunit Phe103alpha mutations on allosteric activation of alternate substrate dioxygenation by vanillin compared to the wild-type enzyme, overview | Sphingobium sp. | |
Vanillin | like the wild-type enzyme, F103T and F103V alpha-subunit point mutants also exhibit allosteric activation for the dioxygenation of protocatechuate and gallate, respectively | Sphingobium sp. |
Application | Comment | Organism |
---|---|---|
biofuel production | enhanced utilization of substrates by enzyme mutants F103T and F103V makes them potentially useful for efforts to develop engineered organisms that catabolize lignin into biofuels or fine chemicals | Sphingobium sp. |
Protein Variants | Comment | Organism |
---|---|---|
F103T | site-directed mutagenesis, mutation in the alpha-subunit, the mutant shows enhanced utilization of substrates gallate and 3-O-methylgallate, but not of protocatechuate, compared to the wild-type enzyme | Sphingobium sp. |
F103V | site-directed mutagenesis, mutation in the alpha-subunit, the mutant shows enhanced utilization of substrates gallate and 3-O-methylgallate, but not of protocatechuate, compared to the wild-type enzyme | Sphingobium sp. |
additional information | in silico docking of substrates to the enzyme mutants, and impact of Phe103alpha mutations on allosteric activation of alternate substrate dioxygenation, overview | Sphingobium sp. |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten steady-state kinetics of wild-type and mutant enzymes | Sphingobium sp. | |
0.051 | - |
protocatechuate | pH 7.5, 25°C, recombinant wild-type enzyme | Sphingobium sp. | |
0.108 | - |
protocatechuate | pH 7.5, 25°C, recombinant mutant F103H | Sphingobium sp. | |
0.19 | - |
gallate | pH 7.5, 25°C, recombinant mutant F103H | Sphingobium sp. | |
0.21 | - |
protocatechuate | pH 7.5, 25°C, recombinant mutant F103T | Sphingobium sp. | |
0.21 | - |
gallate | pH 7.5, 25°C, recombinant mutant F103T | Sphingobium sp. | |
0.26 | - |
protocatechuate | pH 7.5, 25°C, recombinant mutant F103V | Sphingobium sp. | |
0.39 | - |
3-O-methylgallate | pH 7.5, 25°C, recombinant mutant F103T | Sphingobium sp. | |
0.44 | - |
gallate | pH 7.5, 25°C, recombinant wild-type enzyme | Sphingobium sp. | |
0.9 | - |
gallate | pH 7.5, 25°C, recombinant mutant F103V | Sphingobium sp. | |
0.93 | - |
3-O-methylgallate | pH 7.5, 25°C, recombinant mutant F103H | Sphingobium sp. | |
1 | - |
3-O-methylgallate | pH 7.5, 25°C, recombinant mutant F103V | Sphingobium sp. | |
1.6 | - |
protocatechuate | pH 7.5, 25°C, recombinant mutant F103L | Sphingobium sp. | |
2.3 | - |
3-O-methylgallate | pH 7.5, 25°C, recombinant wild-type enzyme | Sphingobium sp. | |
4 | - |
3-O-methylgallate | pH 7.5, 25°C, recombinant mutant F103L | Sphingobium sp. | |
7 | - |
gallate | pH 7.5, 25°C, recombinant mutant F103L | Sphingobium sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
protocatechuate + O2 | Sphingobium sp. | - |
4-carboxy-2-hydroxymuconate semialdehyde | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sphingobium sp. | G2IQQ4 AND G2IQQ3 | alpha- and beta-chain of LigAB; formerly Sphingomonas paucimobilis SYK-6 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-O-methylgallate + O2 | - |
Sphingobium sp. | ? | - |
? | |
gallate + O2 | - |
Sphingobium sp. | ? | - |
? | |
additional information | protocatechuate 4,5-dioxygenase (LigAB) catalyzes dioxygenation of multiple lignin derived aromatic compounds with decreasing efficiency as the molecule size increases. Residue F103 of the alpha-subunit controls substrate specificity through interaction with the C5-funtionality of bound substrates. In silico docking of substrates to the enzyme mutants, overview | Sphingobium sp. | ? | - |
? | |
protocatechuate + O2 | - |
Sphingobium sp. | 4-carboxy-2-hydroxymuconate semialdehyde | - |
? |
Synonyms | Comment | Organism |
---|---|---|
LigAB | - |
Sphingobium sp. |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Sphingobium sp. |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
5 | - |
gallate | pH 7.5, 25°C, recombinant mutant F103L | Sphingobium sp. | |
7 | - |
3-O-methylgallate | pH 7.5, 25°C, recombinant mutant F103L | Sphingobium sp. | |
7.3 | - |
3-O-methylgallate | pH 7.5, 25°C, recombinant wild-type enzyme | Sphingobium sp. | |
15.1 | - |
3-O-methylgallate | pH 7.5, 25°C, recombinant mutant F103T | Sphingobium sp. | |
22.7 | - |
gallate | pH 7.5, 25°C, recombinant mutant F103T | Sphingobium sp. | |
24 | - |
gallate | pH 7.5, 25°C, recombinant mutant F103V | Sphingobium sp. | |
33 | - |
protocatechuate | pH 7.5, 25°C, recombinant mutant F103L | Sphingobium sp. | |
41 | - |
gallate | pH 7.5, 25°C, recombinant mutant F103H | Sphingobium sp. | |
49 | - |
3-O-methylgallate | pH 7.5, 25°C, recombinant mutant F103V | Sphingobium sp. | |
53 | - |
gallate | pH 7.5, 25°C, recombinant wild-type enzyme | Sphingobium sp. | |
89 | - |
protocatechuate | pH 7.5, 25°C, recombinant mutant F103V | Sphingobium sp. | |
91 | - |
3-O-methylgallate | pH 7.5, 25°C, recombinant mutant F103H | Sphingobium sp. | |
110 | - |
protocatechuate | pH 7.5, 25°C, recombinant mutant F103H | Sphingobium sp. | |
112 | - |
protocatechuate | pH 7.5, 25°C, recombinant mutant F103T | Sphingobium sp. | |
216 | - |
protocatechuate | pH 7.5, 25°C, recombinant wild-type enzyme | Sphingobium sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Sphingobium sp. |