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Information on EC 1.1.1.27 - L-lactate dehydrogenase and Organism(s) Plasmodium falciparum

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EC Tree
IUBMB Comments
Also oxidizes other (S)-2-hydroxymonocarboxylic acids. NADP+ also acts, more slowly, with the animal, but not the bacterial, enzyme.
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Select one or more organisms in this record: ?
This record set is specific for:
Plasmodium falciparum
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The taxonomic range for the selected organisms is: Plasmodium falciparum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
hide
(S)-lactate
+
NAD+
=
pyruvate
+
NADH
+
H+
+
=
+
+
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydrogenase, lactate
-
-
-
-
Epsilon crystallin
-
-
-
-
epsilon-crystallin
-
-
-
-
Immunogenic protein p36
-
-
-
-
L(+)-nLDH
-
-
-
-
L-(+)-lactate dehydrogenase
-
-
-
-
L-lactate dehydrogenase
-
L-lactic acid dehydrogenase
-
-
-
-
L-lactic dehydrogenase
-
-
-
-
L-LDH
lactate dehydrogenase
lactate dehydrogenase NAD-dependent
-
-
-
-
lactic acid dehydrogenase
-
-
-
-
lactic dehydrogenase
-
-
-
-
NAD-lactate dehydrogenase
-
-
-
-
PfLDH
proteins, specific or class, anoxic stress response, p34
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
(S)-lactate:NAD+ oxidoreductase
Also oxidizes other (S)-2-hydroxymonocarboxylic acids. NADP+ also acts, more slowly, with the animal, but not the bacterial, enzyme.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-60-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-lactate + 3-acetyl pyridine adenine dinucleotide
pyruvate + reduced 3-acetyl pyridine adenine dinucleotide
show the reaction diagram
-
assay is based on reduction of 3-acetyl pyridine adenine dinucleotide that is specific for PfLDH, which allows the distinction of PfLDH from that of the host erythrocyte
-
-
?
(S)-lactate + 3-acetylpyridine adenine dinucleotide
pyruvate + reduced 3-acetylpyridine adenine dinucleotide
show the reaction diagram
-
-
-
?
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
2-oxobutyrate + NADH
2-hydroxybutyrate + NAD+
show the reaction diagram
-
-
-
-
r
2-oxovalerate + NADH
2-hydroxyvalerate + NAD+
show the reaction diagram
-
-
-
-
r
4-methyl-2-oxopentanoate + NADH
2-hydroxy-4-methylpentanoate + NAD+
show the reaction diagram
-
-
-
-
?
L-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
phenylpyruvate + NADH
2-hydroxy-3-phenylpropanoate + NAD+
show the reaction diagram
-
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
additional information
?
-
-
Plasmodium falciparum lactate dehydrogenase has L-malate dehydrogenase activity, which plays a role in the tricarboxylic acid cycle
-
-
?
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
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
involved in glycolysis
-
-
r
L-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-acetylpyridine adenine dinucleotide
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(abieta-8,11,13-trien-18-ylamino)(oxo)acetic acid
-
-
(benzylamino)(oxo)acetic acid
-
-
(heptylamino)(oxo)acetic acid
-
-
(hexylamino)(oxo)acetic acid
-
-
(nonylamino)(oxo)acetic acid
-
-
([2-cyano-4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]phenyl]amino)(oxo)acetic acid
-
-
([4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]-2-methoxyphenyl]amino)(oxo)acetic acid
-
-
([4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]phenyl]amino)(oxo)acetic acid
-
-
1,6-dibromo-2-hydroxynaphthalene 3-carboxylic acid
-
0.31 mM
1-[7-[3,4-dihydroxy-2-imino-7-methyl-5-(propan-2-yl)-2H-naphtho[1,8-bc]furan-8-yl]-2,3,8-trihydroxy-6-methyl-4-(propan-2-yl)naphthalen-1-yl]ethanone
-
-
2,3-dihydroxy-4,6,7-trimethylnaphthalene-1-carboxylic acid
-
-
2,3-dihydroxy-4,6-dimethylnaphthalene-1-carboxylic acid
-
-
2,3-dihydroxy-6,7-dimethyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
-
2,3-dihydroxy-6,7-dimethyl-4-propylnaphthalene-1-carboxylic acid
-
-
2,3-dihydroxy-6-methyl-4-(propan-2-yl)-7-[4-(trifluoromethyl)benzyl]naphthalene-1-carboxylic acid
-
-
2,3-dihydroxy-6-methyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
-
2,3-dihydroxy-6-methyl-4-propylnaphthalene-1-carboxylic acid
-
-
2,3-dihydroxy-6-methyl-7-(2-methylbenzyl)-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
-
2,3-dihydroxy-6-methyl-7-(3-methylbenzyl)-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
-
2,3-dihydroxy-6-methyl-7-(4-methylbenzyl)-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
-
2,6-naphthalene disulfonic acid
-
IC50: 21 mM
2,6-naphthalenedicarboxalic acid
-
IC50: 5.1 mM
3,5-dihydroxy 2-naphthoic acid
-
IC50: 1.7 mM
3,5-dihydroxynaphthalene-2-carboxylic acid
-
-
3,7-dihydroxy naphthalene-2-carboxylic acid
-
IC50: 2.4 mM
3,7-dihydroxynaphthalene-2-carboxylic acid
-
-
3-(3-nitropyridin-4-yl)-2-oxopropanoic acid
-
-
3-acetylpyridine adenine dinucleotide
-
the enzyme exhibits characteristic reduced substrate inhibition and enhanced kcat
3-hydroxy-1,2-oxazole-4-carboxylic acid
-
-
3-hydroxy-1-oxaspiro[4.5]dec-3-en-2-one
-
-
4,7-dibromo-3-hydroxynaphthalene-2-carboxylic acid
-
-
4-(ethylcarbamoyl)benzoic acid
-
-
4-hydroxy-1,2,5-oxadiazole-3-carboxylic acid
4-hydroxy-1,2,5-thiadiazole-3-carboxylic acid
-
-
4-hydroxy-1,2-oxazole-3-carboxylic acid
-
-
6,6'-disulfanediyldipyridine-3-carboxylic acid
-
-
6,6'-Dithiodinicotinic acid
-
IC50: 6.6 mM
7-(4-chlorobenzyl)-2,3-dihydroxy-6-methyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
-
7-benzyl-2,3-dihydroxy-4,6-dimethylnaphthalene-1-carboxylic acid
-
-
7-benzyl-2,3-dihydroxy-6-methyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
-
7-benzyl-2,3-dihydroxy-6-methyl-4-propylnaphthalene-1-carboxylic acid
-
-
8'-acetyl-1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalene-8-carboxylic acid
-
-
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl acetate
-
-
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl butanoate
-
-
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl pentanoate
-
-
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl propanoate
-
-
8-(2-[4-[(carboxycarbonyl)amino]-3-methoxyphenyl]ethoxy)-5-hydroxy-4-oxo-4H-chromene-2-carboxylic acid
-
-
8-(phenylamino)naphthalene-1-sulfonic acid
-
-
8-([4-[(carboxycarbonyl)amino]-3-methoxybenzyl]oxy)-5-hydroxy-4-oxo-4H-chromene-2-carboxylic acid
-
-
8-anilino-1-naphthalene sulfonic acid
-
IC50: 0.52 mM
8-[8-acetyl-1,6,7-trihydroxy-3-methyl-5-(propan-2-yl)naphthalen-2-yl]-3,4-dihydroxy-7-methyl-5-(propan-2-yl)-2H-naphtho[1,8-bc]furan-2-one
-
-
amino(oxo)acetic acid
-
-
bis(acetatato-kO)(biphenyl-2,2'-diyl-k2C2,C2')copper
-
-
bis(acetatato-kO)(biphenyl-2,2'-diyl-k2C2,C2')zinc
-
-
Chloroquine
ethyl 3-(3-cyanopyridin-4-yl)-2-oxopropanoate
-
-
gossylic nitrile 1,1'-diacetate
-
gossypol
gossypol lactone
-
L-lactate
-
product inhibition
NAD+
-
product inhibition
naphthalene-2,6-dicarboxylic acid
-
-
naphthalene-2,6-disulfonic acid
-
-
oxo(pentadecylamino)acetic acid
-
-
oxo(phenylamino)acetic acid
-
-
oxo[(2-phenylethyl)amino]acetic acid
-
-
oxo[(2-phenylpropyl)amino]acetic acid
-
-
oxo[(3-phenylpropyl)amino]acetic acid
-
-
oxo[(4-phenylbutan-2-yl)amino]acetic acid
-
-
oxo[(4-phenylbutyl)amino]acetic acid
-
-
oxo[(tetrahydrofuran-2-ylmethyl)amino]acetic acid
-
-
oxo[[1-(5,6,7,8-tetrahydronaphthalen-1-yl)ethyl]amino]acetic acid
-
-
pyruvate
[(2-ethylphenyl)(phenyl)amino](oxo)acetic acid
-
-
[(2-methoxyethyl)amino](oxo)acetic acid
-
-
[(3,3-diphenylpropyl)amino](oxo)acetic acid
-
-
[(3-methoxypropyl)amino](oxo)acetic acid
-
-
[(3-methylbutyl)amino](oxo)acetic acid
-
-
[(3-methylphenyl)(phenyl)amino](oxo)acetic acid
-
-
[(4-chlorobenzyl)amino](oxo)acetic acid
-
-
[(4-methylbenzyl)amino](oxo)acetic acid
-
-
[(furan-2-ylmethyl)(methyl)amino](oxo)acetic acid
-
-
[(naphthalen-1-ylmethyl)amino](oxo)acetic acid
-
-
[benzyl(methyl)amino](oxo)acetic acid
-
-
[bis(2-methylpiperidin-1-yl)amino](oxo)acetic acid
-
-
[bis(4-benzylpiperazin-1-yl)amino](oxo)acetic acid
-
-
[bis(4-benzylpiperidin-1-yl)amino](oxo)acetic acid
-
-
[bis(4-phenylpiperazin-1-yl)amino](oxo)acetic acid
-
-
[[2-(4-bromophenyl)ethyl]amino](oxo)acetic acid
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12
(S)-lactate
pH 9.2, 25°C
0.6
2-oxobutyrate
-
pH 7.5
0.116
2-oxovalerate
-
pH 7.5
0.123
3-acetylpyridine adenine dinucleotide
pH 9.2, 25°C
0.047
L-lactate
-
pH 7.5
0.086 - 0.18
NAD+
0.007 - 0.065
NADH
0.03 - 0.055
pyruvate
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
65
(S)-lactate
pH 9.2, 25°C
80
2-oxobutyrate
-
pH 7.5
0.64
2-oxovalerate
-
pH 7.5
250
3-acetylpyridine adenine dinucleotide
pH 9.2, 25°C
0.33
4-methyl-2-oxopentanoate
-
wild-type enzyme
40
L-lactate
-
pH 7.5
40 - 65
NAD+
96 - 148.3
NADH
39.5
phenylpyruvate
-
wild-type enzyme
94 - 180
pyruvate
additional information
additional information
-
turnover-numbers for mutant enzymes with enlarged loop
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.016
1-[7-[3,4-dihydroxy-2-imino-7-methyl-5-(propan-2-yl)-2H-naphtho[1,8-bc]furan-8-yl]-2,3,8-trihydroxy-6-methyl-4-(propan-2-yl)naphthalen-1-yl]ethanone
-
pH not specified in the publication, temperature not specified in the publication
0.013
2,3-dihydroxy-4,6,7-trimethylnaphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.022
2,3-dihydroxy-4,6-dimethylnaphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.001
2,3-dihydroxy-6,7-dimethyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.0001
2,3-dihydroxy-6,7-dimethyl-4-propylnaphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.0002
2,3-dihydroxy-6-methyl-4-(propan-2-yl)-7-[4-(trifluoromethyl)benzyl]naphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.002
2,3-dihydroxy-6-methyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.006
2,3-dihydroxy-6-methyl-4-propylnaphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.008
7-benzyl-2,3-dihydroxy-4,6-dimethylnaphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.0007
7-benzyl-2,3-dihydroxy-6-methyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.0003
7-benzyl-2,3-dihydroxy-6-methyl-4-propylnaphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.0012
8'-acetyl-1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalene-8-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.0008
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl acetate
-
pH not specified in the publication, temperature not specified in the publication
0.0006
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl butanoate
-
pH not specified in the publication, temperature not specified in the publication
0.0003
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl pentanoate
-
pH not specified in the publication, temperature not specified in the publication
0.0011
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl propanoate
-
pH not specified in the publication, temperature not specified in the publication
0.0004
8-[8-acetyl-1,6,7-trihydroxy-3-methyl-5-(propan-2-yl)naphthalen-2-yl]-3,4-dihydroxy-7-methyl-5-(propan-2-yl)-2H-naphtho[1,8-bc]furan-2-one
-
pH not specified in the publication, temperature not specified in the publication
0.0007
gossylic nitrile 1,1'-diacetate
pH 7.5, 25°C
0.0007
gossypol
0.0004
gossypol lactone
pH 7.5, 25°C
0.14 - 57
pyruvate
additional information
additional information
-
substrate and product inhibition kinetics
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.059
(abieta-8,11,13-trien-18-ylamino)(oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.00008
(benzylamino)(oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.16
(heptylamino)(oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.047
(hexylamino)(oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.088
(nonylamino)(oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.0083
([2-cyano-4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]phenyl]amino)(oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.00175
([4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]-2-methoxyphenyl]amino)(oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.0031
([4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]phenyl]amino)(oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
21
2,6-naphthalene disulfonic acid
Plasmodium falciparum
-
IC50: 21 mM
5.1
2,6-naphthalenedicarboxalic acid
Plasmodium falciparum
-
IC50: 5.1 mM
1.7
3,5-dihydroxy 2-naphthoic acid
Plasmodium falciparum
-
IC50: 1.7 mM
1.7
3,5-dihydroxynaphthalene-2-carboxylic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
2.4
3,7-dihydroxy naphthalene-2-carboxylic acid
Plasmodium falciparum
-
IC50: 2.4 mM
2.4
3,7-dihydroxynaphthalene-2-carboxylic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.0011
3-hydroxy-1,2-oxazole-4-carboxylic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.31
4,7-dibromo-3-hydroxynaphthalene-2-carboxylic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.00065
4-hydroxy-1,2,5-oxadiazole-3-carboxylic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.00014
4-hydroxy-1,2,5-thiadiazole-3-carboxylic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.016
4-hydroxy-1,2-oxazole-3-carboxylic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
6.6
6,6'-disulfanediyldipyridine-3-carboxylic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
6.6
6,6'-Dithiodinicotinic acid
Plasmodium falciparum
-
IC50: 6.6 mM
0.191
8-(2-[4-[(carboxycarbonyl)amino]-3-methoxyphenyl]ethoxy)-5-hydroxy-4-oxo-4H-chromene-2-carboxylic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.52
8-(phenylamino)naphthalene-1-sulfonic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.0873
8-([4-[(carboxycarbonyl)amino]-3-methoxybenzyl]oxy)-5-hydroxy-4-oxo-4H-chromene-2-carboxylic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.52
8-anilino-1-naphthalene sulfonic acid
Plasmodium falciparum
-
IC50: 0.52 mM
0.0944
amino(oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
5.5
Chloroquine
Plasmodium falciparum
-
IC50: 5.5 mM
5.11
naphthalene-2,6-dicarboxylic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
21
naphthalene-2,6-disulfonic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.2
oxo(pentadecylamino)acetic acid
Plasmodium falciparum
-
above, pH not specified in the publication, temperature not specified in the publication
0.0001
oxo[(2-phenylethyl)amino]acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.000035
oxo[(3-phenylpropyl)amino]acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.041
oxo[(4-phenylbutyl)amino]acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.0188
oxo[(tetrahydrofuran-2-ylmethyl)amino]acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.146
oxo[[1-(5,6,7,8-tetrahydronaphthalen-1-yl)ethyl]amino]acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.2
[(2-ethylphenyl)(phenyl)amino](oxo)acetic acid
Plasmodium falciparum
-
above, pH not specified in the publication, temperature not specified in the publication
0.014
[(2-methoxyethyl)amino](oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.035
[(3,3-diphenylpropyl)amino](oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.043
[(3-methoxypropyl)amino](oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.157
[(3-methylbutyl)amino](oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.0979
[(3-methylphenyl)(phenyl)amino](oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.00007
[(4-chlorobenzyl)amino](oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.00009
[(4-methylbenzyl)amino](oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.2
[(furan-2-ylmethyl)(methyl)amino](oxo)acetic acid
Plasmodium falciparum
-
above, pH not specified in the publication, temperature not specified in the publication
0.043
[(naphthalen-1-ylmethyl)amino](oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.2
[benzyl(methyl)amino](oxo)acetic acid
Plasmodium falciparum
-
above, pH not specified in the publication, temperature not specified in the publication
0.2
[bis(2-methylpiperidin-1-yl)amino](oxo)acetic acid
Plasmodium falciparum
-
above, pH not specified in the publication, temperature not specified in the publication
0.169
[bis(4-benzylpiperazin-1-yl)amino](oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.101
[bis(4-benzylpiperidin-1-yl)amino](oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.2
[bis(4-phenylpiperazin-1-yl)amino](oxo)acetic acid
Plasmodium falciparum
-
above, pH not specified in the publication, temperature not specified in the publication
0.051
[[2-(4-bromophenyl)ethyl]amino](oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
253
reduction of pyruvate
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
the recombinant protein is exclusively associated with inclusion bodies
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
the parasite's ATP production is almost completely dependent on the glucose metabolism and the glycolytic pathway, that is absent in normal human host cells, overview. PfLDH plays the essential role in NAD+ regenration needed for the continuity of the glycolytic cycle
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LDH_PLAFA
42
0
4955
Swiss-Prot
other Location (Reliability: 1)
Q71T02_PLAFA
316
0
34108
TrEMBL
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
Rossmann fold topology, structure comparison to the enzyme from Homo sapiens, PDB IDs 1i10 and 1ldg, differences occur mainly in the N-terminus, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals the apo-form of PfLDH are ontained by hanging-drop method with 2-methyl-2,4-pentanediol as precipitant, crystallization of enzyme:naphthoic acid complexes with 2,6-naphthalenedicarboxalic acid, 2,6-naphthalene disulfonic acid or 3,7-dihydroxy naphthalene-2-carboxylic acid and 3,7-dihydroxy naphthalene-2-carboxylic acid plus NAD+
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N197D
-
1.15fold increase in activity, 2.7fold increase in kcat/Km ratio, 2fold increase in production titer for asymmetric synthesis of (S)-2-hydroxybutanoic acid
S163L
-
decrease in substrate inhibition, the Km value for pyruvate is increased substantially and the turnover number is 60% that of wild type
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
half-life of wild-type is 50.4 h, of mutant N197D is 77.9 h
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to homogeneity yielding 18 mg of protein/litre culture
-
wild-type and enlarged loop mutants ELM1 and ELM2
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene pfldh, recombinant expression in Saccharomyces cerevisiae, the optimized engineered strain is used as host for L-lactic acid fermentation. Strain IBB10B05 incorporates a NADH-dependent pathway for oxidoreductive xylose assimilation within CEN.PK113-7D background and is additionally evolved for accelerated xylose-to-ethanol fermentation. The pfldh gene is placed in strain IBB10B05 at the pdc1 locus under control of the pdc1 promotor, and strain IBB14LA1_5 additionally has the pdc5 gene disrupted resulting in strain IBB14LA1. The Saccharomyces cerevisiae strain originally optimized for xylose-to-ethanol fermentation is useful to implement L-lactic acid production from glucose and xylose
into pQE-30 Xa vector and expressed in Escherichia coli SG13009 cells
-
the single gene encoding the enzyme is located on chromosome 13
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is induced at 37°C by 0.5 mM beta-D-thiogalactoside concentration being associated with inclusion bodies. By reducing cell growth temperature to 15°C and sopropyl beta-D-thiogalactoside concentration to 0.25 mM, it is possible to get approximately 82% of expressed protein in soluble form
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
medicine
potential drug target for new antimalarials
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hewitt, C.O.; Sessions, R.B.; Dafforn, T.R.; Holbrook, J.J.
Protein engineering tests of a homology model of Plasmodium falciparum lactate dehydrogenase
Protein Eng.
10
39-44
1997
Plasmodium falciparum
Manually annotated by BRENDA team
Brown, W.M.; Yowell, C.A.; Hoard, A.; vander Jagt, T.A.; Hunsaker, L.A.; Deck, L.M.; Royer, R.E.; Piper, R.C.; Dame, J.B.; Makler, M.T.; vander Jagt, D.L.
Comparative structural analysis and kinetic properties of lactate dehydrogenases from the four species of human Malarial parasites
Biochemistry
43
6219-6229
2004
Plasmodium malariae, Plasmodium ovale, Plasmodium falciparum (Q27743), Plasmodium falciparum, Plasmodium vivax (Q6JH30), Plasmodium vivax
Manually annotated by BRENDA team
Winter, V.J.; Cameron, A.; Tranter, R.; Sessions, R.B.; Brady, R.L.
Crystal structure of Plasmodium berghei lactate dehydrogenase indicates the unique structural differences of these enzymes are shared across the Plasmodium genus
Mol. Biochem. Parasitol.
131
1-10
2003
Plasmodium berghei, Plasmodium falciparum
Manually annotated by BRENDA team
Vivas, L.; Easton, A.; Kendrick, H.; Cameron, A.; Lavandera, J.L.; Barros, D.; de las Heras, F.G.; Brady, R.L.; Croft, S.L.
Plasmodium falciparum: stage specific effects of a selective inhibitor of lactate dehydrogenase
Exp. Parasitol.
111
105-114
2005
Plasmodium falciparum
Manually annotated by BRENDA team
Conners, R.; Schambach, F.; Read, J.; Cameron, A.; Sessions, R.B.; Vivas, L.; Easton, A.; Croft, S.L.; Brady, R.L.
Mapping the binding site for gossypol-like inhibitors of Plasmodium falciparum lactate dehydrogenase
Mol. Biochem. Parasitol.
142
137-148
2005
Plasmodium falciparum
Manually annotated by BRENDA team
Wiwanitkit, V.
Plasmodium and host lactate dehydrogenase molecular function and biological pathways: implication for antimalarial drug discovery
Chem. Biol. Drug Des.
69
280-283
2007
Plasmodium falciparum
Manually annotated by BRENDA team
Shoemark, D.K.; Cliff, M.J.; Sessions, R.B.; Clarke, A.R.
Enzymatic properties of the lactate dehydrogenase enzyme from Plasmodium falciparum
FEBS J.
274
2738-2748
2007
Plasmodium falciparum
Manually annotated by BRENDA team
Berwal, R.; Gopalan, N.; Chandel, K.; Prasad, G.B.; Prakash, S.
Plasmodium falciparum: enhanced soluble expression, purification and biochemical characterization of lactate dehydrogenase
Exp. Parasitol.
120
135-141
2008
Plasmodium falciparum
Manually annotated by BRENDA team
Granchi, C.; Bertini, S.; Macchia, M.; Minutolo, F.
Inhibitors of lactate dehydrogenase isoforms and their therapeutic potentials
Curr. Med. Chem.
17
672-697
2010
Bos taurus, Homo sapiens, Plasmodium falciparum, Plasmodium vivax, Plasmodium malariae, Plasmodium ovale
Manually annotated by BRENDA team
Novy, V.; Brunner, B.; Mueller, G.; Nidetzky, B.
Toward homolactic fermentation of glucose and xylose by engineered Saccharomyces cerevisiae harboring a kinetically efficient L-lactate dehydrogenase within pdc1-pdc5 deletion background
Biotechnol. Bioeng.
114
163-171
2017
Plasmodium falciparum (Q27743), Plasmodium falciparum
Manually annotated by BRENDA team
Tian, L.; Zhou, J.; Lv, Q.; Liu, F.; Yang, T.; Zhang, X.; Xu, M.; Rao, Z.
Rational engineering of the Plasmodium falciparum L-lactate dehydrogenase loop involved in catalytic proton transfer to improve chiral 2-hydroxybutyric acid production
Int. J. Biol. Macromol.
179
71-79
2021
Plasmodium falciparum
Manually annotated by BRENDA team