EC Number |
Protein Variants |
Reference |
---|
5.3.1.16 | D127F |
mutation generates phosphoribosylanthranilate isomerase activity |
662618 |
5.3.1.16 | D127G |
mutation generates phosphoribosylanthranilate isomerase activity |
662618 |
5.3.1.16 | D127K |
mutation generates phosphoribosylanthranilate isomerase activity |
662618 |
5.3.1.16 | D127N |
turnover number for NĀ-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 2481fold higher than that of the wild-type enzyme. The Km-value for NĀ-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 3.3fold higher than that of the wild-type enzyme |
648892 |
5.3.1.16 | D127T |
mutation generates phosphoribosylanthranilate isomerase activity |
662618 |
5.3.1.16 | D127V |
mutation generates phosphoribosylanthranilate isomerase activity |
662618 |
5.3.1.16 | D127V/T164H |
mutation generates phosphoribosylanthranilate isomerase activity |
662618 |
5.3.1.16 | D51N |
turnover number for NĀ-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 2.3fold higher than that of the wild-type enzyme. The Km-value for NĀ-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 9.4fold higher than that of the wild-type enzyme |
648892 |
5.3.1.16 | D7N |
residue D7 acts as the catalytic base, crystallization data |
-, 748198 |
5.3.1.16 | D7N/D176A |
residue D7 acts as the catalytic base, and D176 acts as the catalytic acid, crystallization data |
-, 748198 |