We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments Also oxidizes other (S)-2-hydroxymonocarboxylic acids. NADP+ also acts, more slowly, with the animal, but not the bacterial, enzyme.
The taxonomic range for the selected organisms is: Toxoplasma gondii The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
lactate dehydrogenase, lactic dehydrogenase, ldh-a, lactate dehydrogenase a, l-lactate dehydrogenase, ldh-5, lactic acid dehydrogenase, ldh-1, pfldh, alpha-hydroxybutyrate dehydrogenase,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dehydrogenase, lactate
-
-
-
-
Epsilon crystallin
-
-
-
-
epsilon-crystallin
-
-
-
-
Immunogenic protein p36
-
-
-
-
L-(+)-lactate dehydrogenase
-
-
-
-
L-lactic acid dehydrogenase
-
-
-
-
L-lactic dehydrogenase
-
-
-
-
lactate dehydrogenase NAD-dependent
-
-
-
-
lactic acid dehydrogenase
-
-
-
-
lactic dehydrogenase
-
-
-
-
NAD-lactate dehydrogenase
-
-
-
-
proteins, specific or class, anoxic stress response, p34
-
-
-
-
lactate dehydrogenase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(S)-lactate:NAD+ oxidoreductase
Also oxidizes other (S)-2-hydroxymonocarboxylic acids. NADP+ also acts, more slowly, with the animal, but not the bacterial, enzyme.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pyruvate + NADH
L-lactate + NAD+
LDH2 has an important physiological function, in addition to being a glycolytic enzyme and differentiation marker. The enzymatic activity, growth, and virulence of tachyzoites are unaffected by the presence of the recombinant protein. Overexpression of LDH2 enhances the parasite's ability to differentiate
-
-
?
pyruvate + NADH
L-lactate + NAD+
LDH1 has an important physiological function, in addition to being a glycolytic enzyme and differentiation marker. The enzymatic activity, growth, and virulence of tachyzoites are unaffected by the presence of the recombinant protein. Overexpression of LDH1 enhances the parasite's ability to differentiate
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
pyruvate + NADH + H+
(S)-lactate + NAD+
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
terminal enzyme in aerobic glycolysis necessary for NAD+ regeneration
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pyruvate + NADH + H+
(S)-lactate + NAD+
terminal enzyme in aerobic glycolysis necessary for NAD+ regeneration
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
under alkaline conditions the presence of the recombinant LDH proteins increases the differentiation
additional information
under alkaline conditions the presence of the recombinant LDH proteins increases the differentiation
additional information
-
under alkaline conditions the presence of the recombinant LDH proteins increases the differentiation
additional information
under alkaline conditions the presence of the recombinant LDH protein increases the differentiation
additional information
under alkaline conditions the presence of the recombinant LDH protein increases the differentiation
additional information
-
under alkaline conditions the presence of the recombinant LDH protein increases the differentiation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LDH2
brenda
-
brenda
additional information
LDH2 is absent from tachyzoites
brenda
additional information
LDH2 is absent from tachyzoites
brenda
additional information
-
LDH2 is absent from tachyzoites
brenda
additional information
LDH1 is absent from bradyzoites
brenda
additional information
LDH1 is absent from bradyzoites
brenda
additional information
-
LDH1 is absent from bradyzoites
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
brenda
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LDH_TOXGO
326
0
35307
Swiss-Prot
other Location (Reliability: 5 )
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
in apo-form and in ternary complexes containing NAD+ or NAD+-analogue 3-acetylpyridine adenine dinucleotide and sulfate or the inhibitor oxalate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
into expression plasmid pTUB8Myc-His-X-HX under the control of a modified tubulin promoter. Type I strain of Toxoplasma gondii RHDELTAHX transformed with plasmid. Transgenic parasites overexpressing LDH2
expression in Escherichia coli
into expression plasmid pTUB8Myc-His-X-HX under the control of a modified tubulin promoter. Type I strain of Toxoplasma gondii RHDELTAHX transformed with plasmid. Transgenic parasites overexpressing LDH1
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
medicine
structural characterization of the enzyme and active-site differences from the human lactate dehydrogenase may be useful for structural-based design of new treatments for toxoplasmic infections
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Kavanagh, K.L.; Elling, R.A.; Wilson, D.K.
Structure of Toxoplasma gondii LDH1: active-site differences from human lactate dehydrogenases and the structural basis for efficient APAD+ use
Biochemistry
43
879-889
2004
Toxoplasma gondii (P90613), Toxoplasma gondii
brenda
Liwak, U.; Ananvoranich, S.
Toxoplasma gondii: Over-expression of lactate dehydrogenase enhances differentiation under alkaline conditions
Exp. Parasitol.
122
155-161
2009
Toxoplasma gondii (P90613), Toxoplasma gondii (Q27797), Toxoplasma gondii
brenda