Crystallization (Comment) | Organism |
---|---|
in complex with transition state analogues | Vibrio cholerae |
Protein Variants | Comment | Organism |
---|---|---|
A113P | mutation of Vibrio cholera MTAN catalytic site residue to match those of Escherichia coli MTAN, about 4fold decrease in catalytic efficiency | Vibrio cholerae |
A113P/V153I | mutation of Vibrio cholera MTAN catalytic site residues to match those of Escherichia coli MTAN. In the Val153Ile mutant or double mutants, transition-state analogue binding at one site causes complete inhibition. Amino acid, Val153, alters the catalytic site cooperativity in MTAN | Vibrio cholerae |
V153I | mutatition of Vibrio cholera MTAN catalytic site residues to match those of Escherichia coli MTAN. In the Val153Ile mutant or double mutants, transition-state analogue binding at one site causes complete inhibition. Amino acid, Val153, alters the catalytic site cooperativity in MTAN | Vibrio cholerae |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
(3R,4S)-1-[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[(butylsulfanyl)methyl]pyrrolidin-3-ol | - |
Vibrio cholerae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.000061 | - |
S-adenosyl-L-homocysteine | wild-type, pH 7.7, temperature not specified in the publication | Vibrio cholerae | |
0.000202 | - |
S-adenosyl-L-homocysteine | mutant A113P/V153I, pH 7.7, temperature not specified in the publication | Vibrio cholerae | |
0.000262 | - |
S-adenosyl-L-homocysteine | mutant A113P, pH 7.7, temperature not specified in the publication | Vibrio cholerae | |
0.00043 | - |
S-adenosyl-L-homocysteine | mutant V153I, pH 7.7, temperature not specified in the publication | Vibrio cholerae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Vibrio cholerae | A5F5R2 | - |
- |
Vibrio cholerae ATCC 39541 | A5F5R2 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
S-adenosyl-L-homocysteine + H2O | - |
Vibrio cholerae | S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine | - |
? | |
S-adenosyl-L-homocysteine + H2O | - |
Vibrio cholerae ATCC 39541 | S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine | - |
? |
Synonyms | Comment | Organism |
---|---|---|
MTAN | - |
Vibrio cholerae |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0079 | - |
S-adenosyl-L-homocysteine | mutant V153I, pH 7.7, temperature not specified in the publication | Vibrio cholerae | |
0.17 | - |
S-adenosyl-L-homocysteine | mutant A113P, pH 7.7, temperature not specified in the publication | Vibrio cholerae | |
0.18 | - |
S-adenosyl-L-homocysteine | wild-type, pH 7.7, temperature not specified in the publication | Vibrio cholerae | |
0.4 | - |
S-adenosyl-L-homocysteine | mutant A113P/V153I, pH 7.7, temperature not specified in the publication | Vibrio cholerae |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
18 | - |
S-adenosyl-L-homocysteine | mutant V153I, pH 7.7, temperature not specified in the publication | Vibrio cholerae | |
400 | - |
S-adenosyl-L-homocysteine | mutant A113P/V153I, pH 7.7, temperature not specified in the publication | Vibrio cholerae | |
700 | - |
S-adenosyl-L-homocysteine | mutant A113P, pH 7.7, temperature not specified in the publication | Vibrio cholerae | |
3000 | - |
S-adenosyl-L-homocysteine | wild-type, pH 7.7, temperature not specified in the publication | Vibrio cholerae |