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Literature summary 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

Protein Variants

EC Number Protein Variants Comment Organism
1.13.11.81 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
1.13.11.81 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
4.1.2.25 Y53F the mutation converts the enzyme to a cofactor-independent oxygenase, which generates mainly 7,8-dihydroxanthopterin Escherichia coli
4.1.2.25 Y54F the mutation converts the enzyme to a cofactor-independent oxygenase, which generates mainly 7,8-dihydroxanthopterin Staphylococcus aureus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.11.81 7,8-dihydroneopterin + O2 Staphylococcus aureus
-
7,8-dihydroxanthopterin + formate + glycolaldehyde
-
?
1.13.11.81 7,8-dihydroneopterin + O2 Escherichia coli
-
7,8-dihydroxanthopterin + formate + glycolaldehyde
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.81 Escherichia coli P0AC16
-
-
1.13.11.81 Staphylococcus aureus
-
-
-
4.1.2.25 Escherichia coli
-
-
-
4.1.2.25 Staphylococcus aureus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.2.25 DEAE-cellulose column chromatography and Bio-Gel A-0.5m gel filtration Escherichia coli
4.1.2.25 Ni-NTA column chromatography and Bio-Gel A-0.5m gel filtration Staphylococcus aureus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.81 7,8-dihydroneopterin + O2
-
Staphylococcus aureus 7,8-dihydroxanthopterin + formate + glycolaldehyde
-
?
1.13.11.81 7,8-dihydroneopterin + O2
-
Escherichia coli 7,8-dihydroxanthopterin + formate + glycolaldehyde
-
?
4.1.2.25 7,8-dihydroneopterin
-
Staphylococcus aureus 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
?
4.1.2.25 7,8-dihydroneopterin
-
Escherichia coli 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
?

Synonyms

EC Number Synonyms Comment Organism
1.13.11.81 dihydroneopterin oxygenase
-
Staphylococcus aureus
1.13.11.81 dihydroneopterin oxygenase
-
Escherichia coli
1.13.11.81 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
1.13.11.81 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
4.1.2.25 DHNA
-
Staphylococcus aureus
4.1.2.25 DHNA
-
Escherichia coli

Cofactor

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