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Information on EC 1.5.99.14 - 6-hydroxypseudooxynicotine dehydrogenase and Organism(s) Paenarthrobacter nicotinovorans and UniProt Accession Q93NH4

for references in articles please use BRENDA:EC1.5.99.14
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IUBMB Comments
Contains a cytidylyl molybdenum cofactor . The enzyme, which participates in the nicotine degradation pathway, has been characterized from the soil bacterium Arthrobacter nicotinovorans [1,2].
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This record set is specific for:
Paenarthrobacter nicotinovorans
UNIPROT: Q93NH4
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The taxonomic range for the selected organisms is: Paenarthrobacter nicotinovorans
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
6-hydroxypseudooxynicotine dehydrogenase, more
SYSTEMATIC NAME
IUBMB Comments
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one:acceptor 6-oxidoreductase (hydroxylating)
Contains a cytidylyl molybdenum cofactor [3]. The enzyme, which participates in the nicotine degradation pathway, has been characterized from the soil bacterium Arthrobacter nicotinovorans [1,2].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + phenazine methosulfate + H2O
1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one + reduced phenazine methosulfate
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
molybdopterin cytosine dinucleotide
cofactor is required for assembly of the heterotrimeric molybdenum enzyme
iron-sulfur centre
presence of two [Fe2-S2] centers
molybdopterin cytosine dinucleotide
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0125 - 0.065
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.3 - 10.58
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
80 - 720
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
encoded on megaplasmid pAO1
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HLNO_PAENI
425
0
46335
Swiss-Prot
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of the Kdh holoenzyme, with its three subunits KdhL, KdhM, and KdhS, and their associated cofactors molybdopterin cytosine dinucleotide, two iron-sulfur clusters (Fe2S2), and flavin adenine dinucleotide, respectively. The residues Glu345, Try551, and Glu748 of KdhL participate in substrate binding, and Phe269 and Arg383 of KdhL contribute to stabilize the molybdopterin cytosine dinucleotide conformation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E345A
mutation in subunit KdhL, inactive
E748A
mutation in subunit KdhL, inactive
F269A
mutation in subunit KdhL, 8fold decrease in catalytic efficiency
R383A
mutation in subunit KdhL, 2fold decrease in catalytic efficiency
W551A
mutation in subunit KdhL, inactive
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sachelaru, P.; Schiltz, E.; Brandsch, R.
A functional mobA gene for molybdopterin cytosine dinucleotide cofactor biosynthesis is required for activity and holoenzyme assembly of the heterotrimeric nicotine dehydrogenases of Arthrobacter nicotinovorans
Appl. Environ. Microbiol.
72
5126-5131
2006
Paenarthrobacter nicotinovorans (Q93NH4)
Manually annotated by BRENDA team
Wang, L.; Mu, X.; Li, W.; Xu, Q.; Xu, P.; Zhang, L.; Zhang, Y.; Wu, G.
Structural, mechanistic, and functional insights into an Arthrobacter nicotinovorans molybdenum hydroxylase involved in nicotine degradation
Molecules
26
4387
2021
Paenarthrobacter nicotinovorans (O87681 and O87682 and Q933N0)
Manually annotated by BRENDA team