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5.3.1.16: 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase

This is an abbreviated version!
For detailed information about 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase, go to the full flat file.

Word Map on EC 5.3.1.16

Reaction

1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
=
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide

Synonyms

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ketol-isomerase, 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase, BBM II isomerase, BBM II ketolisomerase, BBMII isomerase, eHisA, HisA, Isomerase, N-(phosphoribosylformimino) aminophosphoribosylimidazolecarboxamide, Isomerase, phosphoribosylformiminoaminophosphoribosylimidazolecarboxamide, N'-[(5'-phosphoribosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide isomerase, phosphoribosyl-5-amino-1-phosphoribosyl-4-imidazolecarboxamide isomerase, Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, ProFAR isomerase, tHisA

ECTree

     5 Isomerases
         5.3 Intramolecular oxidoreductases
             5.3.1 Interconverting aldoses and ketoses, and related compounds
                5.3.1.16 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase

Engineering

Engineering on EC 5.3.1.16 - 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D7N
residue D7 acts as the catalytic base, crystallization data
D7N/D176A
residue D7 acts as the catalytic base, and D176 acts as the catalytic acid, crystallization data
D7N
-
residue D7 acts as the catalytic base, crystallization data
-
D7N/D176A
-
residue D7 acts as the catalytic base, and D176 acts as the catalytic acid, crystallization data
-
D127F
-
mutation generates phosphoribosylanthranilate isomerase activity
D127G
-
mutation generates phosphoribosylanthranilate isomerase activity
D127K
-
mutation generates phosphoribosylanthranilate isomerase activity
D127N
-
turnover number for N‘-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 2481fold higher than that of the wild-type enzyme. The Km-value for N‘-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 3.3fold higher than that of the wild-type enzyme
D127T
-
mutation generates phosphoribosylanthranilate isomerase activity
D127V
-
mutation generates phosphoribosylanthranilate isomerase activity
D127V/T164H
-
mutation generates phosphoribosylanthranilate isomerase activity
D51N
-
turnover number for N‘-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 2.3fold higher than that of the wild-type enzyme. The Km-value for N‘-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 9.4fold higher than that of the wild-type enzyme
D8N
-
activity with N‘-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is immeasurable low
H48A
-
turnover number for N‘-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 1.8fold lower than that of the wild-type enzyme. The Km-value for N‘-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 4.8fold lower than that of the wild-type enzyme
R83N
-
turnover number for N‘-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 2.9fold higher than that of the wild-type enzyme. The Km-value for N‘-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 63.2fold higher than that of the wild-type enzyme
T164A
-
turnover number for N‘-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 37.2fold higher than that of the wild-type enzyme. The Km-value for N‘-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 9.3fold higher than that of the wild-type enzyme