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Literature summary for 1.13.11.81 extracted from

  • Wang, Y.; Scherperel, G.; Roberts, K.D.; Jones, A.D.; Reid, G.E.; Yan, H.
    A point mutation converts dihydroneopterin aldolase to a cofactor-independent oxygenase (2006), J. Am. Chem. Soc., 128, 13216-13223.
    View publication on PubMed
Search for more literature for 1.13.11.81

Protein Variants

Protein Variants Comment Organism
Y53F the substitution of a conserved tyrosine residue at the active site of dihydroneopterin aldolase by phenylalanine converts the enzyme to a cofactor-independent oxygenase, which generates mainly 7,8-dihydroxanthopterin rather than 6-hydroxymethyl-7,8-dihydropterin Escherichia coli
Y54F the substitution of a conserved tyrosine residue at the active site of dihydroneopterin aldolase by phenylalanine converts the enzyme to a cofactor-independent oxygenase, which generates mainly 7,8-dihydroxanthopterin rather than 6-hydroxymethyl-7,8-dihydropterin Staphylococcus aureus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7,8-dihydroneopterin + O2 Staphylococcus aureus
-
 7,8-dihydroxanthopterin + formate + glycolaldehyde
-
 ?
7,8-dihydroneopterin + O2 Escherichia coli
-
 7,8-dihydroxanthopterin + formate + glycolaldehyde
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AC16
-
-
Staphylococcus aureus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7,8-dihydroneopterin + O2
-
 Staphylococcus aureus 7,8-dihydroxanthopterin + formate + glycolaldehyde
-
 ?
7,8-dihydroneopterin + O2
-
 Escherichia coli 7,8-dihydroxanthopterin + formate + glycolaldehyde
-
 ?

Synonyms

Synonyms Comment Organism
dihydroneopterin oxygenase
-
 Staphylococcus aureus
dihydroneopterin oxygenase
-
 Escherichia coli
Y53F mutant of dihydroneopterin aldolase substitution of a conserved tyrosine residue at the active site of dihydroneopterin aldolase by phenylalanine converts the enzyme to a cofactor-independent oxygenase, which generates mainly 7,8-dihydroxanthopterin rather than 6-hydroxymethyl-7,8-dihydropterin Escherichia coli
Y54F mutant of dihydroneopterin aldolase substitution of a conserved tyrosine residue at the active site of dihydroneopterin aldolase by phenylalanine converts the enzyme to a cofactor-independent oxygenase, which generates mainly 7,8-dihydroxanthopterin rather than 6-hydroxymethyl-7,8-dihydropterin Staphylococcus aureus

Cofactor

Cofactor Comment Organism Structure
additional information cofactor-independent Staphylococcus aureus
additional information cofactor-independent Escherichia coli