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Literature summary for 5.3.1.24 extracted from

  • Noda-Garcia, L.; Camacho-Zarco, A.R.; Verdel-Aranda, K.; Wright, H.; Soberon, X.; Fueloep, V.; Barona-Gomez, F.
    Identification and analysis of residues contained on beta --> alpha loops of the dual-substrate (beta alpha)8 phosphoribosyl isomerase A specific for its phosphoribosyl anthranilate isomerase activity (2010), Protein Sci., 19, 535-543.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
into the vector pET-15b Streptomyces coelicolor

Crystallization (Commentary)

Crystallization (Comment) Organism
the structure of the PriA mutant R139N is determined to a resolution of 1.95 A Streptomyces coelicolor

Protein Variants

Protein Variants Comment Organism
R139N mutant, used for crystallization, steady-state Michaelis-Menten enzyme kinetic is studied Streptomyces coelicolor
R19A mutant, steady-state Michaelis-Menten enzyme kinetic is studied Streptomyces coelicolor
S81T mutant, steady-state Michaelis-Menten enzyme kinetic is studied Streptomyces coelicolor

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.004
-
N-(5-phospho-beta-D-ribosyl)anthranilate PriA, PRA isomerase activity Streptomyces coelicolor
0.005
-
N-(5-phospho-beta-D-ribosyl)anthranilate PriA, PRA isomerase activity Streptomyces coelicolor
0.0083
-
N-(5-phospho-beta-D-ribosyl)anthranilate PriA mutant R19A, PRA isomerase activity Streptomyces coelicolor

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N-(5-phospho-beta-D-ribosyl)anthranilate Streptomyces coelicolor
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
?

Organism

Organism UniProt Comment Textmining
Streptomyces coelicolor P16250
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Streptomyces coelicolor

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-(5-phospho-beta-D-ribosyl)anthranilate
-
Streptomyces coelicolor 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
?

Synonyms

Synonyms Comment Organism
phosphoribosyl anthranilate isomerase
-
Streptomyces coelicolor
phosphoribosyl isomerase A
-
Streptomyces coelicolor
PRA isomerase
-
Streptomyces coelicolor
PriA
-
Streptomyces coelicolor

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
activity assay Streptomyces coelicolor

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.4
-
N-(5-phospho-beta-D-ribosyl)anthranilate PriA mutant R19A, PRA isomerase activity Streptomyces coelicolor
3.4
-
N-(5-phospho-beta-D-ribosyl)anthranilate PriA, PRA isomerase activity Streptomyces coelicolor
12
-
N-(5-phospho-beta-D-ribosyl)anthranilate PriA, PRA isomerase activity Streptomyces coelicolor

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
activity assay Streptomyces coelicolor

General Information

General Information Comment Organism
metabolism phosphoribosyl isomerase A takes part in histidine and tryptophan biosynthesis Streptomyces coelicolor