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Information on EC 1.13.11.54 - acireductone dioxygenase [iron(II)-requiring] and Organism(s) Mus musculus and UniProt Accession Q99JT9

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IUBMB Comments
Requires iron(II). If Ni2+ is bound instead of iron(II), the reaction catalysed by EC 1.13.11.53, acireductone dioxygenase (Ni2+-requiring), occurs instead. The enzyme from the bacterium Klebsiella oxytoca (formerly Klebsiella pneumoniae) ATCC strain 8724 is involved in the methionine salvage pathway.
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Mus musculus
UNIPROT: Q99JT9
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
mtcbp-1, osard1, fe-ard, 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
if Fe+2 is bound in the active site, the substrate acireductone reacts with O2 to yield formate and 3-(methylthio)propanoate
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one:oxygen oxidoreductase (formate-forming)
Requires iron(II). If Ni2+ is bound instead of iron(II), the reaction catalysed by EC 1.13.11.53, acireductone dioxygenase (Ni2+-requiring), occurs instead. The enzyme from the bacterium Klebsiella oxytoca (formerly Klebsiella pneumoniae) ATCC strain 8724 is involved in the methionine salvage pathway.
CAS REGISTRY NUMBER
COMMENTARY hide
221681-63-6
-
221681-64-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(1Z)-1,2-dihydroxyhex-1-en-3-one + O2
2-oxovalerate + formic acid
show the reaction diagram
i.e. desthio-acireductone
-
-
?
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
3-(methylthio)propanoate + formate + CO
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
the Ni2+ bound protein catalyzes the reaction of EC 1.13.11.53
Mn2+
the Ni2+ bound protein catalyzes the reaction of EC 1.13.11.53
Ni2+
the Ni2+ bound protein catalyzes the reaction of EC 1.13.11.53
additional information
the identity of bound metal ion does not affect the oligomeric state of ARD
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1185
(1Z)-1,2-dihydroxyhex-1-en-3-one
Fe2+ bound enzyme, pH 7.0, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
111.7
(1Z)-1,2-dihydroxyhex-1-en-3-one
Fe2+ bound enzyme, pH 7.0, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
950
(1Z)-1,2-dihydroxyhex-1-en-3-one
Fe2+ bound enzyme, pH 7.0, 25°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MTND_MOUSE
179
0
21524
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23000 - 26000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni- and Co-bound proteins. Both Ni and Co present an octahedral coordination geometry in the active site bound to protein ligands H88, H90, H133 and E94. Additionally, two distinct water (or hydroxide) ligands bind to the metal ion center
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H98S
mutation results in the formation of a stable soluble protein that while structurally different from ARD shows a high degree of similarity to the ARD' enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43
Mn2+ bound enzyme, melting temperature
58
Ni2+ bound enzyme, melting temperature
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain BL21(DE3)pLysS
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ju, T.; Goldsmith, R.B.; Chai, S.C.; Maroney, M.J.; Pochapsky, S.S.; Pochapsky, T.C.
One protein, two enzymes revisited: A structural entropy switch interconverts the two isoforms of acireductone dioxygenase
J. Mol. Biol.
363
823-834
2006
Mus musculus (Q99JT9)
Manually annotated by BRENDA team
Deshpande, A.R.; Wagenpfeil, K.; Pochapsky, T.C.; Petsko, G.A.; Ringe, D.
Metal-dependent function of a mammalian acireductone dioxygenase
Biochemistry
55
1398-1407
2016
Mus musculus (Q99JT9)
Manually annotated by BRENDA team