Information on EC 1.13.11.81 - 7,8-dihydroneopterin oxygenase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.13.11.81
-
RECOMMENDED NAME
GeneOntology No.
7,8-dihydroneopterin oxygenase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
7,8-dihydroneopterin + O2 = 7,8-dihydroxanthopterin + formate + glycolaldehyde
show the reaction diagram
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
7,8-dihydroneopterin:oxygen oxidoreductase
The enzyme from the bacterium Mycobacterium tuberculosis is multifunctional and also catalyses the epimerisation of the 2'-hydroxy group of 7,8-dihydroneopterin (EC 5.1.99.8, 7,8-dihydroneopterin epimerase) and the reaction of EC 4.1.2.25 (dihydroneopterin aldolase).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
7,8-dihydroneopterin + O2
7,8-dihydroxanthopterin + formate + glycolaldehyde
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
7,8-dihydroneopterin + O2
7,8-dihydroxanthopterin + formate + glycolaldehyde
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000154
7,8-dihydroneopterin
at pH 7.0 and 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0011
7,8-dihydroneopterin
Mycobacterium tuberculosis
P9WNC5
at pH 7.0 and 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.3
7,8-dihydroneopterin
Mycobacterium tuberculosis
P9WNC5
at pH 7.0 and 25°C
3544
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16585
4 * 16585, electrospray ionization mass spectrometry
16716
4 * 16716, calculated from amino acid sequence
62300
sedimentation equilibrium analysis
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
4 * 16585, electrospray ionization mass spectrometry; 4 * 16716, calculated from amino acid sequence
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and Superdex 200 gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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