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Literature summary for 6.3.4.18 extracted from

  • Thoden, J.B.; Holden, H.M.; Paritala, H.; Firestine, S.M.
    Structural and functional studies of Aspergillus clavatus N(5)-carboxyaminoimidazole ribonucleotide synthetase (2010), Biochemistry, 49, 752-760.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
medicine observed only in microorganisms, target for antimicrobial drug Aspergillus clavatus

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli HMS174 cells Aspergillus clavatus

Protein Variants

Protein Variants Comment Organism
D153A mutation without affecting substrate binding but critical role in catalysis, decrease in catalytic proficiency Aspergillus clavatus
E73A mutation with affect on substrate binding, decrease in catalytic proficiency Aspergillus clavatus
K353A mutation without affecting substrate binding but critical role in catalysis, decrease in catalytic proficiency Aspergillus clavatus
R155A mutation with affect on substrate binding, decrease in catalytic proficiency Aspergillus clavatus
Y152A mutation with affect on substrate binding, decrease in catalytic proficiency Aspergillus clavatus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.025
-
5-amino-1-(5-phospho-D-ribosyl)imidazole wild-type enzyme Aspergillus clavatus
0.04
-
5-amino-1-(5-phospho-D-ribosyl)imidazole mutant D153A Aspergillus clavatus
0.14
-
5-amino-1-(5-phospho-D-ribosyl)imidazole mutant E73A Aspergillus clavatus
0.18
-
5-amino-1-(5-phospho-D-ribosyl)imidazole mutant R155A Aspergillus clavatus
0.46
-
5-amino-1-(5-phospho-D-ribosyl)imidazole mutant Y152A Aspergillus clavatus

Organism

Organism UniProt Comment Textmining
Aspergillus clavatus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
standard methods with nickel nitrilotiacetic acid resin Aspergillus clavatus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole + HCO3- assay at pH 7.5, 37°C Aspergillus clavatus ADP + 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + phosphate
-
?

Synonyms

Synonyms Comment Organism
N5-CAIR synthetase
-
Aspergillus clavatus
N5-carboxyaminoimidazole ribonucleotide synthetase
-
Aspergillus clavatus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Aspergillus clavatus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Aspergillus clavatus

General Information

General Information Comment Organism
physiological function key enzyme in microbial de novo purine biosynthesis Aspergillus clavatus

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.67
-
5-amino-1-(5-phospho-D-ribosyl)imidazole mutant E73A Aspergillus clavatus
2
-
5-amino-1-(5-phospho-D-ribosyl)imidazole mutant D153A Aspergillus clavatus
8.3
-
5-amino-1-(5-phospho-D-ribosyl)imidazole mutant Y152A Aspergillus clavatus
100
-
5-amino-1-(5-phospho-D-ribosyl)imidazole mutant R155A Aspergillus clavatus
5500
-
5-amino-1-(5-phospho-D-ribosyl)imidazole wild-type enzyme Aspergillus clavatus