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Literature summary 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

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

Cloned(Commentary)

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

Protein Variants

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.4.18 0.025
-
5-amino-1-(5-phospho-D-ribosyl)imidazole wild-type enzyme Aspergillus clavatus
6.3.4.18 0.04
-
5-amino-1-(5-phospho-D-ribosyl)imidazole mutant D153A Aspergillus clavatus
6.3.4.18 0.14
-
5-amino-1-(5-phospho-D-ribosyl)imidazole mutant E73A Aspergillus clavatus
6.3.4.18 0.18
-
5-amino-1-(5-phospho-D-ribosyl)imidazole mutant R155A Aspergillus clavatus
6.3.4.18 0.46
-
5-amino-1-(5-phospho-D-ribosyl)imidazole mutant Y152A Aspergillus clavatus

Organism

EC Number Organism UniProt Comment Textmining
6.3.4.18 Aspergillus clavatus
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.4.18 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

EC Number Synonyms Comment Organism
6.3.4.18 N5-CAIR synthetase
-
Aspergillus clavatus
6.3.4.18 N5-carboxyaminoimidazole ribonucleotide synthetase
-
Aspergillus clavatus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.3.4.18 37
-
assay at Aspergillus clavatus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.4.18 7.5
-
assay at Aspergillus clavatus

General Information

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

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
6.3.4.18 0.67
-
5-amino-1-(5-phospho-D-ribosyl)imidazole mutant E73A Aspergillus clavatus
6.3.4.18 2
-
5-amino-1-(5-phospho-D-ribosyl)imidazole mutant D153A Aspergillus clavatus
6.3.4.18 8.3
-
5-amino-1-(5-phospho-D-ribosyl)imidazole mutant Y152A Aspergillus clavatus
6.3.4.18 100
-
5-amino-1-(5-phospho-D-ribosyl)imidazole mutant R155A Aspergillus clavatus
6.3.4.18 5500
-
5-amino-1-(5-phospho-D-ribosyl)imidazole wild-type enzyme Aspergillus clavatus