Information on EC 1.14.13.187 - L-evernosamine nitrososynthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.13.187
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RECOMMENDED NAME
GeneOntology No.
L-evernosamine nitrososynthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dTDP-beta-L-evernosamine + 2 NADPH + 2 H+ + 2 O2 = dTDP-2,3,6-trideoxy-3-C-methyl-4-O-methyl-3-nitroso-beta-L-arabino-hexopyranose + 2 NADP+ + 3 H2O
show the reaction diagram
dTDP-beta-L-evernosamine + NADPH + H+ + O2 = dTDP-N-hydroxy-beta-L-evernosamine + NADP+ + H2O
show the reaction diagram
dTDP-N-hydroxy-beta-L-evernosamine + NADPH + H+ + O2 = dTDP-2,3,6-trideoxy-3-C-methyl-4-O-methyl-3-nitroso-beta-L-arabino-hexopyranose + NADP+ + 2 H2O
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
dTDP-beta-L-evernosamine,NADPH:oxygen oxidoreductase (N-hydroxylating)
Requires FAD. Isolated from the bacterium Micromonospora carbonacea var. africana. The nitroso group is probably spontaneously oxidized to a nitro group giving dTDP-beta-L-evernitrose, which is involved in the biosynthesis of the antibiotic everninomycin. The reaction was studied using dTDP-beta-L-4-epi-vancosamine (dTDP-4-O-desmethyl-beta-L-evernitrosamine).
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
in the anthracycline biosynthetic pathway, the enzyme's specific role involves the synthesis of the seven-carbon acetal moiety attached to C4 of l-daunosamine observed in the anthracycline baumycin
physiological function
DnmZ is an N-hydroxylating flavin monooxygenase and a nitrososynthase that catalyzes the oxidation of the exocyclic amine of the sugar nucleotide dTDP-L-epi-vancosamine to its nitroso form. Its specific role in the anthracycline biosynthetic pathway involves the synthesis of the seven-carbon acetal moiety attached to C4 of l-daunosamine observed in the anthracycline baumycin
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dTDP-beta-L-evernosamine + 2 NADPH + 2 H+ + 2 O2
dTDP-2,3,6-trideoxy-3-C-methyl-4-O-methyl-3-nitroso-beta-L-arabino-hexopyranose + 2 NADP+ + 3 H2O
show the reaction diagram
dTDP-beta-L-evernosamine + NADPH + H+ + O2
dTDP-N-hydroxy-beta-L-evernosamine + NADP+ + H2O
show the reaction diagram
dTDP-N-hydroxy-beta-L-evernosamine + NADPH + H+ + O2
dTDP-2,3,6-trideoxy-3-C-methyl-4-O-methyl-3-nitroso-beta-L-arabino-hexopyranose + NADP+ + 2 H2O
show the reaction diagram
TDP-L-epi-vancosamine + 2 NADPH + 2 H+ + 2 O2
? + 2 NADP+ + 3 H2O
show the reaction diagram
additional information
?
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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
dTDP-beta-L-evernosamine + 2 NADPH + 2 H+ + 2 O2
dTDP-2,3,6-trideoxy-3-C-methyl-4-O-methyl-3-nitroso-beta-L-arabino-hexopyranose + 2 NADP+ + 3 H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
dTDP-DnmZ tetramer, crystal structure analysis
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 3.15 A resolution. Tetrameric enzyme that shares a fold with acyl-CoA dehydrogenases and class D flavin-containing monooxygenases, including the nitrososynthase KijD3Enzym displays an unusually open active site. Modeling of FAD and TDP-L-evernosamine into the active site
purified enzyme, hanging drop vapor diffusion method, mixing of 0.001 ml protein solution containing 6 mg/ml of protein DnmZ with 0.001 ml crystallization solution containing 0.05 M glycine pH 9.5, 0.2 M ammonium sulfate, 10% w/v, and PEG 4000, and equilibration against 0.75 ml crystallization solution, 26°C, X-ray diffraction structure determination and analysis at 2.74-3.0 A resolution, molecular replacement using crystal structure PDB ID 3mxl as search model. Cocrystallization of DnmZ complexed with dTDP-L-epi-vancosamine, FAD, FMN or combinations of the amino sugar and flavin are unsuccessful