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Information on EC 1.1.99.6 - D-lactate dehydrogenase (acceptor) and Organism(s) Archaeoglobus fulgidus and UniProt Accession O29853

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IUBMB Comments
The zinc flavoprotein (FAD) from the archaeon Archaeoglobus fulgidus cannot utilize NAD+, cytochrome c, methylene blue or dimethylnaphthoquinone as acceptors. In vitro it is active with artificial electron acceptors such as 2,6-dichlorophenolindophenol, but the physiological acceptor is not yet known.
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Archaeoglobus fulgidus
UNIPROT: O29853
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Word Map
The taxonomic range for the selected organisms is: Archaeoglobus fulgidus
The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
Synonyms
dye-dldh, d-2-hydroxy acid dehydrogenase, dye-linked d-lactate dehydrogenase, dld enzyme, af0394, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-2-hydroxy acid dehydrogenase
-
-
-
-
dehydrogenase, D-2-hydroxy acid
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
-
-
oxidation
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-
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reduction
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-
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-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
(R)-lactate:acceptor 2-oxidoreductase
The zinc flavoprotein (FAD) from the archaeon Archaeoglobus fulgidus cannot utilize NAD+, cytochrome c, methylene blue or dimethylnaphthoquinone as acceptors. In vitro it is active with artificial electron acceptors such as 2,6-dichlorophenolindophenol, but the physiological acceptor is not yet known.
CAS REGISTRY NUMBER
COMMENTARY hide
9028-83-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-lactate + oxidized 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
no activity with L-lactate
-
-
?
(R)-lactate + oxidized 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyl tetrazolium
pyruvate + reduced 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyl tetrazolium
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
the enzyme is expressed constitutively
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
the enzyme contains 1 mol of Zn2+ per mol of protein
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
oxalate
1 mM, addition of Tris buffered oxalate to a reaction mixture inhibits activity
Tris
slight inhibition above 30 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate
stimulates
n-dodecyl beta-D-maltoside
stimulates
phenazine methosulfate
stimulates
Triton X-100
stimulates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15
(R)-lactate
pH 8.5, 60°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
in a 25 mM Tris buffer at 60°C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9.5
pH 7.0: about 30% of maximal activit, pH 9.5: about 55% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 95
25°C: 8% of maximal activity, 95°C: about 75% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
more than 85% of the enzyme is associated with the membrane, integral membrane protein, a significant portion including part of the FAD-binding pocket, is outside the membrane facing the S-layer. NADH oxidase (NoxA2) co-localized to the same sites in the membrane (NoxA2) may protect proteins involved in electron transfer by reducing O2 to H2O2 or H2O
Manually annotated by BRENDA team
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
83
half-life: 105 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression as part of a fusion protein with maltose-binding protein in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pagala, V.R.; Park, J.; Reed, D.W.; Hartzell, P.L.
Cellular localization of D-lactate dehydrogenase and NADH oxidase from Archaeoglobus fulgidus
Archaea
1
95-104
2002
Archaeoglobus fulgidus (O29853)
Manually annotated by BRENDA team
Reed, D.W.; Hartzell, P.L.
The Archaeoglobus fulgidus D-lactate dehydrogenase is a Zn2+ flavoprotein
J. Bacteriol.
181
7580-7587
1999
Archaeoglobus fulgidus (O29853), Archaeoglobus fulgidus
Manually annotated by BRENDA team