EC Number | Crystallization (Comment) | Organism |
---|---|---|
5.3.3.2 | crystal structure of free and metal-bound C67A mutant enzyme | Escherichia coli |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
5.3.3.2 | C67A | inactive mutant enzyme | Escherichia coli |
5.3.3.2 | E116Q | the ratio of maximal velocity to turnover number is 0.09%% of that of the wild-type enzyme | Escherichia coli |
5.3.3.2 | E87Q | the ratio of maximal velocity to turnover number is 0.07% of that of the wild-type enzyme | Escherichia coli |
5.3.3.2 | K55A | the ratio of maximal velocity to turnover number is 66% of that of the wild-type enzyme | Escherichia coli |
5.3.3.2 | K55R | the ratio of maximal velocity to turnover number is 28% of that of the wild-type enzyme | Escherichia coli |
5.3.3.2 | R51K | the ratio of maximal velocity to turnover number is 4.2% of that of the wild-type enzyme | Escherichia coli |
5.3.3.2 | R83K | the ratio of maximal velocity to turnover number is 104% of that of the wild-type enzyme | Escherichia coli |
5.3.3.2 | W161F | the ratio of maximal velocity to turnover number is 0.8% of that of the wild-type enzyme | Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
5.3.3.2 | 0.0008 | - |
isopentenyl diphosphate | mutant enzyme W161F | Escherichia coli | |
5.3.3.2 | 0.003 | - |
isopentenyl diphosphate | mutant enzyme R83K | Escherichia coli | |
5.3.3.2 | 0.0035 | - |
isopentenyl diphosphate | wild-type enzyme | Escherichia coli | |
5.3.3.2 | 0.0115 | - |
isopentenyl diphosphate | mutant enzyme E87Q | Escherichia coli | |
5.3.3.2 | 0.014 | - |
isopentenyl diphosphate | mutant enzyme K55A | Escherichia coli | |
5.3.3.2 | 0.015 | - |
isopentenyl diphosphate | mutant enzyme K55R | Escherichia coli | |
5.3.3.2 | 0.0185 | - |
isopentenyl diphosphate | mutant enzyme R51K | Escherichia coli | |
5.3.3.2 | 0.021 | - |
isopentenyl diphosphate | mutant enzyme E116Q | Escherichia coli |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
5.3.3.2 | Mg2+ | the enzyme requires one Mn2+ or Mg2+ ion to fold in its active conformation, forming a distorted octahedral metal coordination site composed of three histidines and two glutamates and located in the active site | Escherichia coli | |
5.3.3.2 | Mn2+ | the enzyme requires one Mn2+ or Mg2+ ion to fold in its active conformation, forming a distorted octahedral metal coordination site composed of three histidines and two glutamates and located in the active site | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.3.3.2 | isopentenyl diphosphate | Escherichia coli | the enzyme catalyzes a crucial activation step in the isoprenoid biosynthesis pathway | dimethylallyl diphosphate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
5.3.3.2 | Escherichia coli | Q46822 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
5.3.3.2 | - |
Escherichia coli |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
5.3.3.2 | Isopentenyl diphosphate = dimethylallyl diphosphate | catalytic mechanism in which a cysteine initiates the reaction by protonating the carbon-carbon double bond, with the antarafacial rearrangement ultimately achieved by one of the glutamates involved in the metal coordination sphere | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.3.3.2 | isopentenyl diphosphate | - |
Escherichia coli | dimethylallyl diphosphate | - |
? | |
5.3.3.2 | isopentenyl diphosphate | the enzyme catalyzes a crucial activation step in the isoprenoid biosynthesis pathway | Escherichia coli | dimethylallyl diphosphate | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
5.3.3.2 | IPP:DMAPP | - |
Escherichia coli |