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EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
thisa, bbm ii isomerase, phosphoribosyl-5-amino-1-phosphoribosyl-4-imidazolecarboxamide isomerase, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, bbmii isomerase, profar isomerase,
more
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1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ketol-isomerase
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1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase
BBM II ketolisomerase
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Isomerase, N-(phosphoribosylformimino) aminophosphoribosylimidazolecarboxamide
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Isomerase, phosphoribosylformiminoaminophosphoribosylimidazolecarboxamide
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N'-[(5'-phosphoribosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide isomerase
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phosphoribosyl-5-amino-1-phosphoribosyl-4-imidazolecarboxamide isomerase
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Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase
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1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase
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1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase
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1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase
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HisA
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ProFAR isomerase
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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
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
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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
Amadori rearrangement
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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
enzyme catalyzes Amadori rearrangement of a thermolabile aminoaldolase into the corresponding aminoketose, reaction mechanism involving general acid-base catalysis and a Schiff base intermediate is proposed
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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
enzyme catalyzes Amadori rearrangement of a thermolabile aminoaldolase into the corresponding aminoketose, reaction mechanism involving general acid-base catalysis and a Schiff base intermediate is proposed
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intramolecular oxidoreduction
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isomerization
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1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide aldose-ketose-isomerase
Involved in histidine biosynthesis.
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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
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide
5-[(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino]-1-(5-phosphoribosyl)imidazole-4-carboxamide
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
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N-(5'-Phospho-D-ribosylformimino)-5-amino-1-(5''-phospho-D-ribosyl)-4-imidazolecarboxamide
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enzyme catalyzes the fourth step in histidine biosynthesis
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N-(5'-Phospho-D-ribosylformimino)-5-amino-1-(5''-phospho-D-ribosyl)-4-imidazolecarboxamide
N-(5'-Phospho-D-1-ribulosylformimino)-5-amino-1-(5''-phospho-D-ribosyl)-4-imidazolecarboxamide
additional information
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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
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?
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
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?
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide
5-[(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino]-1-(5-phosphoribosyl)imidazole-4-carboxamide
the enzyme catalyzes the fourth step of the His biosynthetic pathway
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1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide
5-[(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino]-1-(5-phosphoribosyl)imidazole-4-carboxamide
ProFAR, aminoaldose
PRFAR, aminoketose
r
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
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N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
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N-(5'-Phospho-D-ribosylformimino)-5-amino-1-(5''-phospho-D-ribosyl)-4-imidazolecarboxamide
N-(5'-Phospho-D-1-ribulosylformimino)-5-amino-1-(5''-phospho-D-ribosyl)-4-imidazolecarboxamide
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N-(5'-Phospho-D-ribosylformimino)-5-amino-1-(5''-phospho-D-ribosyl)-4-imidazolecarboxamide
N-(5'-Phospho-D-1-ribulosylformimino)-5-amino-1-(5''-phospho-D-ribosyl)-4-imidazolecarboxamide
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?
additional information
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APG10 knockout mutant exhibits embryo lethality, indicating the essential role of the Arabidopsis BBMII isomerase for plant growth
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additional information
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APG10 knockout mutant exhibits embryo lethality, indicating the essential role of the Arabidopsis BBMII isomerase for plant growth
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additional information
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enzyme catalyzes Amadori rearrangements of a thermolabile aminoaldolase into the corresponding aminoketose, reaction mechanism involving general acid-base catalysis and a Schiff base intermediate is poposed
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additional information
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the enzyme is involved in histidine biosynthesis
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additional information
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bifunctional enzyme with activity of EC 5.3.1.16 and EC 5.3.1.24
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additional information
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bifunctional enzyme with activity of EC 5.3.1.16 and EC 5.3.1.24 has a dual function in both histidine and aromatic amino acid biosynthesis
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additional information
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bifunctional enzyme with activity of EC 5.3.1.16 and EC 5.3.1.24
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additional information
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bifunctional enzyme with activity of EC 5.3.1.16 and EC 5.3.1.24 has a dual function in both histidine and aromatic amino acid biosynthesis
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additional information
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bifunctional enzyme with activity of EC 5.3.1.16 and EC 5.3.1.24
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additional information
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bifunctional enzyme with activity of EC 5.3.1.16 and EC 5.3.1.24 has a dual function in both histidine and aromatic amino acid biosynthesis
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additional information
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enzyme of histidine biosynthesis
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additional information
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the enzyme is involved in histidine biosynthesis
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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
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide
5-[(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino]-1-(5-phosphoribosyl)imidazole-4-carboxamide
the enzyme catalyzes the fourth step of the His biosynthetic pathway
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N-(5'-Phospho-D-ribosylformimino)-5-amino-1-(5''-phospho-D-ribosyl)-4-imidazolecarboxamide
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enzyme catalyzes the fourth step in histidine biosynthesis
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additional information
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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
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?
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
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additional information
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APG10 knockout mutant exhibits embryo lethality, indicating the essential role of the Arabidopsis BBMII isomerase for plant growth
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additional information
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APG10 knockout mutant exhibits embryo lethality, indicating the essential role of the Arabidopsis BBMII isomerase for plant growth
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additional information
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the enzyme is involved in histidine biosynthesis
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additional information
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bifunctional enzyme with activity of EC 5.3.1.16 and EC 5.3.1.24 has a dual function in both histidine and aromatic amino acid biosynthesis
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additional information
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bifunctional enzyme with activity of EC 5.3.1.16 and EC 5.3.1.24 has a dual function in both histidine and aromatic amino acid biosynthesis
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additional information
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bifunctional enzyme with activity of EC 5.3.1.16 and EC 5.3.1.24 has a dual function in both histidine and aromatic amino acid biosynthesis
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additional information
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enzyme of histidine biosynthesis
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additional information
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the enzyme is involved in histidine biosynthesis
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0.6 - 37.9
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
additional information
additional information
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Km-values for phosphoribosylanthranilate of mutant enzymes D127V, D127K, D127T, D127G, D127F and D127V/T164H
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0.6
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
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25°C or 37°C, pH 7.5, wild-type enzyme
1.6
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
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25°C, pH 7.5
1.8
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
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37°C, pH 7.5
2
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
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25°C, pH 7.5, mutant enzyme D127N
2.9
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
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25°C, pH 7.5, mutant enzyme H48A
5.6
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
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25°C, pH 7.5, mutant enzyme T164A
6.4
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
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25°C, pH 7.5, mutant enzyme D51N
37.9
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
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25°C, pH 7.5, mutant enzyme R83N
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0.00027 - 32
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
additional information
additional information
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turnover-numbers for phosphoribosylanthranilate of mutant enzymes D127V, D127K, D127T, D127G, D127F and D127V/T164H
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0.00027
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
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25°C, pH 7.5, mutant enzyme D127N
0.018
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
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25°C, pH 7.5, mutant enzyme T164A
0.23
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
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25°C, pH 7.5, mutant enzyme R83N
0.29
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
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25°C, pH 7.5, mutant enzyme D51N
0.38
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
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25°C, pH 7.5, mutant enzyme H48A
0.67
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
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25°C, pH 7.5, wild-type enzyme
1.54
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
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37°C, pH 7.5, wild-type enzyme
2.94
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
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37°C, pH 7.5, wild-type enzyme
4.9
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
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25°C, pH 7.5
6.08
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
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25°C, pH 7.5, wild-type enzyme
14.3
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
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37°C, pH 7.5
32
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
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80°C, pH 7.5, wild-type enzyme
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additional information
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brenda
HR37Rv
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HR37Rv
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SWISSPROT
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UniProt
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A3
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SwissProt
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ecotype Columbia
Uniprot
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UniProt
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physiological function
catalytic mechanism involves long loops on the catayltic face that enclose the substrate. Substrate ProFAR adopts an extended conformation where its non-reacting half is in a product-like conformation. This change is associated with shifts in a hydrogen bond network including residues His47, Asp129, Thr171, and Ser202
physiological function
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catalytic mechanism involves long loops on the catayltic face that enclose the substrate. Substrate ProFAR adopts an extended conformation where its non-reacting half is in a product-like conformation. This change is associated with shifts in a hydrogen bond network including residues His47, Asp129, Thr171, and Ser202
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Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Paenarthrobacter aurescens (strain TC1)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
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25600
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analytical ultracentrifugation
25700
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1 * 25700, equilibrium centrifugation of carboxymethlated enzyme in 8 M urea
27400
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analytical ultracentrifugation
27723
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x * 27723, calculation from nucleotide sequence
28400 - 29500
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equilibrium centrifugation
29000
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high speed equilibrium centrifugation
33363
x * 33363, calculation from nucleotide sequence
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x * 33363, calculation from nucleotide sequence
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x * 27723, calculation from nucleotide sequence
monomer
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monomer
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1 * 25700, equilibrium centrifugation of carboxymethlated enzyme in 8 M urea
monomer
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1 * 29000, high speed equilibrium centrifugation of the enzyme after complete reduction and alkylation
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using the anomalous diffraction signal of the protein’s sulfur atoms, enzyme binds a citrate molecule, putative mechanism for the isomerization reaction
wild type in its apo-state and mutants D7N and D7N/D176A in complex with two different conformations of the labile substrate N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide, i.e. ProFAR. Residue D7 acts as the catalytic base, and D176 acts as the catalytic acid
hanging drop vapor diffusion method. All four crystal forms display distinct habits and crystallographic parameters
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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
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residue D7 acts as the catalytic base, crystallization data
D7N/D176A
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residue D7 acts as the catalytic base, and D176 acts as the catalytic acid, crystallization data
D127F
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mutation generates phosporibosylanthranilate isomerase activity
D127G
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mutation generates phosporibosylanthranilate isomerase activity
D127K
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mutation generates phosporibosylanthranilate isomerase activity
D127N
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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
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mutation generates phosporibosylanthranilate isomerase activity
D127V
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mutation generates phosporibosylanthranilate isomerase activity
D127V/T164H
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mutation generates phosporibosylanthranilate isomerase activity
D51N
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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
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activity with N‘-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is immeasurable low
H48A
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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
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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
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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
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40
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10 min, 50% loss of the initial CD signal
95
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10 min, 50% loss of the initial CD signal
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-20°C, stable for several months
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as a his-tagged fusion protein in Saccharomyces cerevisiae
overexpression in Escherichia coli
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the gene complements both hisA and trpF mutants of Escherichia coli
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the gene complements both hisA and trpF mutants of Escherichia coli
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the gene complements both hisA and trpF mutants of Escherichia coli
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Martin, R.G.; Berberich, M.A.; Ames, B.N.; Davis, W.W.; Goldberger, R.F.; Yourno, J.D.
Enzymes and intermediates of histidine biosynthesis in Salmonella typhimurium
Methods Enzymol.
17B
3-44
1971
Salmonella enterica subsp. enterica serovar Typhimurium
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brenda
Margolies, M.N.; Goldberger, R.F.
Physical and chemical characterization of the isomerase of histidine biosynthesis in Salmonella typhimurium
J. Biol. Chem.
242
256-264
1967
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Margolies, M.N.; Goldberger, R.F.
Isolation of the fourth enzyme (isomerase) of histidine biosynthesis from Salmonella typhimurium
J. Biol. Chem.
241
3262-3269
1966
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Henn-Sax, M.; Thoma, R.; Schmidt, S.; Hennig, M.; Kirschner, K.; Sterner, R.
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