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show all sequences of 1.1.1.28

The D-lactate dehydrogenase from Sporolactobacillus inulinus also possessing reversible deamination activity

Zhu, L.; Xu, X.; Wang, L.; Dong, H.; Yu, B.; PLoS ONE 10, e0139066 (2015)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene ldhD, phylogenetic analysis, recombinant expression of wwild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
Sporolactobacillus inulinus
Crystallization (Commentary)
Crystallization
Organism
the complete tertiary structure of DLDH744 in complex with NAD+ is determined, PDB ID 4XKJ, determined by molecular replacement method and refined at 3.15 A-resolution
Sporolactobacillus inulinus
Engineering
Amino acid exchange
Commentary
Organism
E263A
site-directed mutagenesis, the mutant shows highly reduced D-lactate dehydrogenase activity compared to the wild-type enzyme
Sporolactobacillus inulinus
F298A
site-directed mutagenesis, almost inactive D-lactate dehydrogenase mutant
Sporolactobacillus inulinus
G79A
site-directed mutagenesis, almost inactive D-lactate dehydrogenase mutant
Sporolactobacillus inulinus
H295A
site-directed mutagenesis, inactive D-lactate dehydrogenase mutant
Sporolactobacillus inulinus
M307A
site-directed mutagenesisthe mutant shows highly reduced D-lactate dehydrogenase activity compared to the wild-type enzyme
Sporolactobacillus inulinus
additional information
glutamate dehydrogenase activities of enzyme mutants, overview
Sporolactobacillus inulinus
R234A
site-directed mutagenesis, inactive D-lactate dehydrogenase mutant
Sporolactobacillus inulinus
Y101A
site-directed mutagenesis, the mutant shows 50% reduced D-lactate dehydrogenase activity compared to the wild-type enzyme
Sporolactobacillus inulinus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.32
-
phenylpyruvate
recombinant enzyme, pH and temperature not specified in the publication
Sporolactobacillus inulinus
3.4
-
pyruvate
recombinant enzyme, pH and temperature not specified in the publication
Sporolactobacillus inulinus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Sporolactobacillus inulinus
A0A0M3KL04
-
-
Sporolactobacillus inulinus CASD
A0A0M3KL04
-
-
Reaction
Reaction
Commentary
Organism
(R)-lactate + NAD+ = pyruvate + NADH + H+
catalytic mechanism
Sporolactobacillus inulinus
Specific Activity [micromol/min/mg]
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
7.5
-
purified recombinant enzyme, pH and temperature not specified in the publication
Sporolactobacillus inulinus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-lactate + NAD(P)+
the enzyme is confirmed to be a typical D-lactate dehydrogenase based on the activity detected with substrate pyruvate and coenzyme NAD(P)H
741246
Sporolactobacillus inulinus
pyruvate + NAD(P)H + H+
-
-
-
r
(R)-lactate + NAD(P)+
the enzyme is confirmed to be a typical D-lactate dehydrogenase based on the activity detected with substrate pyruvate and coenzyme NAD(P)H
741246
Sporolactobacillus inulinus CASD
pyruvate + NAD(P)H + H+
-
-
-
r
additional information
the bifunctional enzyme from Sporolactobacillus inulinus has both the D-LDH and NAD(P)+/NAD(P)H-utilizing glutamate dehydrogenase (GDH, EC 1.4.1.3) activities, the latter with reversible deamination. Identification of key residues from the crystal structure analysis and site-directed mutagenesis, enzyme reidues Arg234 and Gly79 residues play a significant role in both D-LDH and GDH activities. Residues His295 and Phe298 in DLDH744 are identified to be key residues for lactate dehydrogenase (LDH) activity only, whereas Tyr101 is a unique residue that is critical for GDH activity. DLDH744 is a strict D-2-hydroxyacid dehydrogenase, no formation of L-isomers
741246
Sporolactobacillus inulinus
?
-
-
-
-
additional information
the bifunctional enzyme from Sporolactobacillus inulinus has both the D-LDH and NAD(P)+/NAD(P)H-utilizing glutamate dehydrogenase (GDH, EC 1.4.1.3) activities, the latter with reversible deamination. Identification of key residues from the crystal structure analysis and site-directed mutagenesis, enzyme reidues Arg234 and Gly79 residues play a significant role in both D-LDH and GDH activities. Residues His295 and Phe298 in DLDH744 are identified to be key residues for lactate dehydrogenase (LDH) activity only, whereas Tyr101 is a unique residue that is critical for GDH activity. DLDH744 is a strict D-2-hydroxyacid dehydrogenase, no formation of L-isomers
741246
Sporolactobacillus inulinus CASD
?
-
-
-
-
phenylpyruvate + NADH + H+
-
741246
Sporolactobacillus inulinus
D-phenyllactate + NAD+
-
-
-
r
phenylpyruvate + NADH + H+
-
741246
Sporolactobacillus inulinus CASD
D-phenyllactate + NAD+
-
-
-
r
pyruvate + NAD(P)H + H+
-
741246
Sporolactobacillus inulinus
(R)-lactate + NAD(P)+
-
-
-
r
pyruvate + NAD(P)H + H+
-
741246
Sporolactobacillus inulinus CASD
(R)-lactate + NAD(P)+
-
-
-
r
Subunits
Subunits
Commentary
Organism
homodimer
two identical monomers of DLDH744 are associated at the cofactor binding domain to form the homodimer in one asymmetric unit. The dimer interface is stabilized mainly by hydrogen-bonding interactions between residues from alpha-helices, alpha5(Ser102-Arg119), alpa6(Leu121-Glu130), alpha12(Glu279-Arg285) and connecting loops, structure analysis, overview. His295 is supposed to function as the internal acid-base catalyst in dehydrogenase activity. Glu263 stabilizes the protonated form of His295, and Arg234 forms a hydrogen bond with the nicotinamide ribose ring
Sporolactobacillus inulinus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
512.2
-
pyruvate
recombinant enzyme, pH and temperature not specified in the publication
Sporolactobacillus inulinus
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Sporolactobacillus inulinus
NADH
-
Sporolactobacillus inulinus
NADP+
-
Sporolactobacillus inulinus
NADPH
-
Sporolactobacillus inulinus
Cloned(Commentary) (protein specific)
Commentary
Organism
gene ldhD, phylogenetic analysis, recombinant expression of wwild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
Sporolactobacillus inulinus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Sporolactobacillus inulinus
NADH
-
Sporolactobacillus inulinus
NADP+
-
Sporolactobacillus inulinus
NADPH
-
Sporolactobacillus inulinus
Crystallization (Commentary) (protein specific)
Crystallization
Organism
the complete tertiary structure of DLDH744 in complex with NAD+ is determined, PDB ID 4XKJ, determined by molecular replacement method and refined at 3.15 A-resolution
Sporolactobacillus inulinus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
E263A
site-directed mutagenesis, the mutant shows highly reduced D-lactate dehydrogenase activity compared to the wild-type enzyme
Sporolactobacillus inulinus
F298A
site-directed mutagenesis, almost inactive D-lactate dehydrogenase mutant
Sporolactobacillus inulinus
G79A
site-directed mutagenesis, almost inactive D-lactate dehydrogenase mutant
Sporolactobacillus inulinus
H295A
site-directed mutagenesis, inactive D-lactate dehydrogenase mutant
Sporolactobacillus inulinus
M307A
site-directed mutagenesisthe mutant shows highly reduced D-lactate dehydrogenase activity compared to the wild-type enzyme
Sporolactobacillus inulinus
additional information
glutamate dehydrogenase activities of enzyme mutants, overview
Sporolactobacillus inulinus
R234A
site-directed mutagenesis, inactive D-lactate dehydrogenase mutant
Sporolactobacillus inulinus
Y101A
site-directed mutagenesis, the mutant shows 50% reduced D-lactate dehydrogenase activity compared to the wild-type enzyme
Sporolactobacillus inulinus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.32
-
phenylpyruvate
recombinant enzyme, pH and temperature not specified in the publication
Sporolactobacillus inulinus
3.4
-
pyruvate
recombinant enzyme, pH and temperature not specified in the publication
Sporolactobacillus inulinus
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
7.5
-
purified recombinant enzyme, pH and temperature not specified in the publication
Sporolactobacillus inulinus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-lactate + NAD(P)+
the enzyme is confirmed to be a typical D-lactate dehydrogenase based on the activity detected with substrate pyruvate and coenzyme NAD(P)H
741246
Sporolactobacillus inulinus
pyruvate + NAD(P)H + H+
-
-
-
r
(R)-lactate + NAD(P)+
the enzyme is confirmed to be a typical D-lactate dehydrogenase based on the activity detected with substrate pyruvate and coenzyme NAD(P)H
741246
Sporolactobacillus inulinus CASD
pyruvate + NAD(P)H + H+
-
-
-
r
additional information
the bifunctional enzyme from Sporolactobacillus inulinus has both the D-LDH and NAD(P)+/NAD(P)H-utilizing glutamate dehydrogenase (GDH, EC 1.4.1.3) activities, the latter with reversible deamination. Identification of key residues from the crystal structure analysis and site-directed mutagenesis, enzyme reidues Arg234 and Gly79 residues play a significant role in both D-LDH and GDH activities. Residues His295 and Phe298 in DLDH744 are identified to be key residues for lactate dehydrogenase (LDH) activity only, whereas Tyr101 is a unique residue that is critical for GDH activity. DLDH744 is a strict D-2-hydroxyacid dehydrogenase, no formation of L-isomers
741246
Sporolactobacillus inulinus
?
-
-
-
-
additional information
the bifunctional enzyme from Sporolactobacillus inulinus has both the D-LDH and NAD(P)+/NAD(P)H-utilizing glutamate dehydrogenase (GDH, EC 1.4.1.3) activities, the latter with reversible deamination. Identification of key residues from the crystal structure analysis and site-directed mutagenesis, enzyme reidues Arg234 and Gly79 residues play a significant role in both D-LDH and GDH activities. Residues His295 and Phe298 in DLDH744 are identified to be key residues for lactate dehydrogenase (LDH) activity only, whereas Tyr101 is a unique residue that is critical for GDH activity. DLDH744 is a strict D-2-hydroxyacid dehydrogenase, no formation of L-isomers
741246
Sporolactobacillus inulinus CASD
?
-
-
-
-
phenylpyruvate + NADH + H+
-
741246
Sporolactobacillus inulinus
D-phenyllactate + NAD+
-
-
-
r
phenylpyruvate + NADH + H+
-
741246
Sporolactobacillus inulinus CASD
D-phenyllactate + NAD+
-
-
-
r
pyruvate + NAD(P)H + H+
-
741246
Sporolactobacillus inulinus
(R)-lactate + NAD(P)+
-
-
-
r
pyruvate + NAD(P)H + H+
-
741246
Sporolactobacillus inulinus CASD
(R)-lactate + NAD(P)+
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
two identical monomers of DLDH744 are associated at the cofactor binding domain to form the homodimer in one asymmetric unit. The dimer interface is stabilized mainly by hydrogen-bonding interactions between residues from alpha-helices, alpha5(Ser102-Arg119), alpa6(Leu121-Glu130), alpha12(Glu279-Arg285) and connecting loops, structure analysis, overview. His295 is supposed to function as the internal acid-base catalyst in dehydrogenase activity. Glu263 stabilizes the protonated form of His295, and Arg234 forms a hydrogen bond with the nicotinamide ribose ring
Sporolactobacillus inulinus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
512.2
-
pyruvate
recombinant enzyme, pH and temperature not specified in the publication
Sporolactobacillus inulinus
General Information
General Information
Commentary
Organism
evolution
the enzyme belongs to the D-isomer-specific 2-hydroxyacid dehydrogenase family
Sporolactobacillus inulinus
General Information (protein specific)
General Information
Commentary
Organism
evolution
the enzyme belongs to the D-isomer-specific 2-hydroxyacid dehydrogenase family
Sporolactobacillus inulinus
Other publictions for EC 1.1.1.28
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [░C]
Temperature Range [░C]
Temperature Stability [░C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [░C] (protein specific)
Temperature Range [░C] (protein specific)
Temperature Stability [░C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
739831
Yao
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Efficient biosynthesis of (R)- ...
Staphylococcus epidermidis, Staphylococcus epidermidis ATCC 12228
Adv. Synth. Catal.
358
2923-2928
2016
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-
1
-
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2
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2
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3
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2
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1
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1
1
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2
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2
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2
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-
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-
740314
Li
Carbon flux trapping: highly e ...
Thermodesulfatator indicus
ChemBioChem
17
1491-1494
2016
-
1
1
-
1
-
-
-
-
2
-
1
-
1
-
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1
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6
1
1
1
-
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1
1
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1
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1
1
1
-
1
-
-
-
-
-
-
2
-
1
-
-
-
-
-
-
1
-
6
1
1
1
-
-
1
1
-
-
-
-
-
-
-
-
740225
Zhu
Enhancement of phenyllactic ac ...
Lactobacillus pentosus
Biotechnol. Lett.
37
1233-1241
2015
-
-
1
-
3
-
-
-
-
-
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2
-
3
-
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3
-
1
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1
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2
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1
2
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3
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2
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3
-
1
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1
-
-
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-
1
1
-
-
-
740891
Chen
Development of an enzymatic as ...
Rattus norvegicus, Rattus norvegicus Wistar
J. Pharm. Biomed. Anal.
116
150-155
2015
-
-
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-
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2
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3
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1
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4
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1
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1
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3
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3
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-
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2
-
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1
-
-
4
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
741246
Zhu
The D-lactate dehydrogenase fr ...
Sporolactobacillus inulinus, Sporolactobacillus inulinus CASD
PLoS ONE
10
e0139066
2015
-
-
1
1
8
-
-
2
-
-
-
-
-
3
-
-
-
1
-
-
1
-
8
1
-
-
-
1
-
-
-
4
-
-
-
-
-
1
4
1
8
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
-
8
1
-
-
-
1
-
-
-
-
-
1
1
-
-
-
739810
Kim
Cloning, expression, purificat ...
Lactobacillus jensenii
Acta Crystallogr. Sect. F
70
1046-1048
2014
-
1
1
1
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
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-
-
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-
1
1
-
1
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-
-
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-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
739841
Furukawa
Diverse allosteric and catalyt ...
Escherichia coli, Fusobacterium nucleatum subsp. nucleatum, Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / JCM14847, Pseudomonas aeruginosa
AMB Express
4
76
2014
3
-
3
-
-
-
9
46
-
2
7
3
-
8
-
-
3
3
-
-
-
-
34
4
3
-
3
41
3
-
3
6
10
-
-
3
-
3
6
-
-
-
-
9
10
46
-
2
7
3
-
-
-
3
-
-
-
-
34
4
3
-
3
41
3
-
3
-
-
6
6
-
44
44
739905
Wang
Major role of NAD-dependent la ...
Bacillus coagulans, Bacillus coagulans 2-6, Lactobacillus delbrueckii subsp. bulgaricus, Lactobacillus delbrueckii subsp. bulgaricus DSM 20081, Lactobacillus plantarum subsp. plantarum, Lactobacillus plantarum subsp. plantarum DSM 20174
Appl. Environ. Microbiol.
80
7134-7141
2014
-
-
3
-
-
-
-
4
-
-
-
8
-
11
-
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3
-
-
3
3
-
8
-
3
-
-
4
3
-
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6
-
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-
-
3
6
-
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-
4
-
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8
-
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3
-
3
3
-
8
-
3
-
-
4
3
-
-
-
-
3
3
-
4
4
740223
Yu
Enzymatic production of D-3-ph ...
Pediococcus pentosaceus
Biotechnol. Lett.
36
627-631
2014
-
1
1
-
1
-
1
-
-
-
-
3
-
5
-
-
1
-
-
-
-
-
4
-
1
1
-
-
1
1
-
2
-
-
-
-
1
1
2
-
1
-
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1
-
-
-
-
-
3
-
-
-
1
-
-
-
-
4
-
1
1
-
-
1
1
-
-
-
-
-
-
-
-
741291
Sheng
Efficient production of (R)-2- ...
Lactobacillus delbrueckii subsp. bulgaricus, Lactobacillus delbrueckii subsp. bulgaricus ATCC 1184
PLoS ONE
9
e104204
2014
-
-
1
-
1
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
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2
-
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1
-
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1
-
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-
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1
1
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1
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2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
723678
Jun
-
Discovery and characterization ...
Lactobacillus jensenii
Process Biochem.
48
109-117
2013
-
-
1
-
-
-
-
6
-
-
-
1
-
1
-
-
-
-
-
-
15
-
6
-
2
2
4
6
2
2
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
6
-
-
-
1
-
-
-
-
-
-
15
-
6
-
2
2
4
6
2
2
-
-
-
-
-
-
6
6
740170
Singhvi
Supplementation of medium with ...
Lactobacillus delbrueckii subsp. lactis, Lactobacillus delbrueckii subsp. lactis DSM 20072
Biores. Technol.
146
736-739
2013
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
1
1
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1
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1
1
-
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-
-
-
-
-
1
-
-
-
1
-
-
1
-
-
741405
Zheng
Highly stereoselective biosynt ...
Lactobacillus delbrueckii subsp. bulgaricus, Lactobacillus delbrueckii subsp. bulgaricus ATCC 11842
Sci. Rep.
3
3401
2013
-
-
1
-
4
-
-
4
-
-
-
4
-
4
-
-
1
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-
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-
-
11
-
1
-
-
4
1
-
-
-
-
-
-
-
4
4
721879
Yu
Characterization of D-lactate ...
Pediococcus pentosaceus, Pediococcus pentosaceus ATCC 25745
Biosci. Biotechnol. Biochem.
76
853-855
2012
-
-
-
-
-
-
3
2
-
4
1
4
-
4
-
-
-
-
-
-
2
-
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1
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-
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1
1
1
1
2
1
1
-
-
-
-
-
-
2
2
721909
Mu
Characterization of D-lactate ...
Pediococcus acidilactici, Pediococcus acidilactici DSM 20284
Biotechnol. Lett.
34
907-911
2012
-
-
1
-
-
-
2
2
-
2
1
4
-
2
-
-
1
-
-
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1
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-
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-
4
1
1
1
1
1
1
1
-
-
-
-
-
-
2
2
722140
Li
Characterization of the major ...
Leuconostoc mesenteroides subsp. mesenteroides, Leuconostoc mesenteroides subsp. mesenteroides ATCC 8293
Enzyme Microb. Technol.
51
274-279
2012
-
-
1
-
-
-
3
4
-
-
-
2
-
6
-
-
1
-
-
-
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-
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-
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-
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1
2
1
-
2
2
2
-
-
-
-
-
-
-
-
722283
Wienstroer
D-Lactate dehydrogenase as a m ...
Arabidopsis thaliana, Arabidopsis thaliana Columbia-0
FEBS Lett.
586
36-40
2012
-
1
-
-
1
-
-
-
-
-
-
2
-
5
-
-
-
-
-
2
-
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-
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2
-
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-
-
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-
-
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-
-
-
-
-
721200
Shibahara
Crystallization and preliminar ...
Aeropyrum pernix
Acta Crystallogr. Sect. F
67
1425-1427
2011
-
-
1
1
-
-
-
-
-
-
2
2
-
1
-
-
1
-
-
-
-
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1
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2
1
-
-
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-
-
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-
-
-
-
-
701818
Okano
Improved production of homo-D- ...
Lactobacillus plantarum, Lactobacillus plantarum NCIMB 8826
Appl. Environ. Microbiol.
75
7858-7861
2009
-
-
-
-
1
-
-
-
-
-
-
3
-
5
-
-
-
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-
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3
-
-
-
-
-
-
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-
-
1
1
-
-
-
710727
Antonyuk
Structure of D-lactate dehydro ...
Aquifex aeolicus
Acta Crystallogr. Sect. F
65
1209-1213
2009
-
-
1
1
-
-
-
-
-
-
-
1
-
3
-
-
1
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1
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1
-
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-
-
-
-
-
-
-
1
1
-
-
-
684633
Okino
Production of D-lactic acid by ...
Escherichia coli, Lactobacillus delbrueckii
Appl. Microbiol. Biotechnol.
78
449-454
2008
-
-
2
-
-
-
-
-
-
4
-
2
-
5
-
-
-
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-
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2
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2
-
4
-
-
-
-
-
2
-
-
-
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-
-
-
-
-
695707
Xu
Breeding of D(-)-lactic acid h ...
Sporolactobacillus sp., Sporolactobacillus sp. DX12
Appl. Biochem. Biotechnol.
160
314-321
2008
-
-
-
-
1
-
-
-
-
-
-
2
-
2
-
-
-
-
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4
-
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-
-
-
-
-
-
-
-
-
-
-
688878
Mazzei
-
Peroxidase based biosensors fo ...
Staphylococcus epidermidis
Microchem. J.
87
81-86
2007
-
1
-
-
1
-
-
-
-
1
-
1
-
1
-
-
-
-
-
1
1
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1
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1
-
1
-
-
-
1
-
-
-
-
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-
-
-
667751
Minenko
Use of the addressing sequence ...
Saccharomyces cerevisiae
Biochemistry
71
32-38
2006
-
-
1
-
-
-
-
-
2
-
-
-
-
2
-
-
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-
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-
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-
-
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-
-
-
-
-
-
-
-
-
-
669543
Ishida
D-lactic acid production by me ...
Leuconostoc mesenteroides
J. Biosci. Bioeng.
101
172-177
2006
-
1
1
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
665878
Fujisawa
-
D-lactate metabolism in starve ...
Amphioctopus fangsiao
J. Exp. Zool. A
303A
489-496
2005
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
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-
-
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-
-
-
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-
-
-
-
668233
Findrik
-
Modelling and optimization of ...
Lactobacillus leichmannii
Chem. Biochem. Eng. Q.
19
351-358
2005
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
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1
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-
-
-
-
-
-
-
-
-
-
-
-
669152
Ishikura
Recognition site for the side ...
Lactobacillus pentosus
J. Biochem.
138
741-749
2005
-
-
-
-
9
-
-
46
-
-
-
-
-
2
-
-
-
-
-
-
-
-
10
-
-
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-
46
-
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9
-
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-
10
-
-
-
-
46
-
-
-
-
-
-
-
-
-
-
669327
Shinoda
Distinct conformation-mediated ...
Lactobacillus pentosus
J. Biol. Chem.
280
17068-17075
2005
-
-
-
1
-
-
2
8
-
-
-
-
-
3
-
-
-
-
-
-
-
-
4
-
-
-
-
8
-
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-
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-
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4
8
-
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-
-
4
-
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-
-
8
-
-
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-
-
-
-
-
-
-
670130
Zhu
Effect of a single-gene knocko ...
Escherichia coli
Metab. Eng.
7
104-115
2005
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
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-
-
1
-
-
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-
-
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-
-
-
-
-
-
-
-
-
654456
Hachiya
Interaction of D-lactate dehyd ...
Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
319
78-82
2004
-
-
-
-
1
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
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-
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-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
655064
Horikiri
Electron acquisition system co ...
Rhodopseudomonas palustris
Biosci. Biotechnol. Biochem.
68
516-522
2004
-
-
-
-
-
-
1
1
-
-
2
-
-
2
-
-
1
-
-
-
1
-
3
1
1
-
2
-
1
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2
1
1
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-
-
-
2
-
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-
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1
1
1
-
-
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-
-
-
-
1
-
-
1
-
3
1
1
-
2
-
1
-
-
1
-
-
-
-
-
-
656426
Iino
The effect of sodium acetate o ...
Lactobacillus plantarum, Lactobacillus plantarum 39 / NRIC 1067 / ATCC 14917 / DSM 20174, Lactobacillus sakei, Lactobacillus sakei NRIC 1071 / ATCC 15521 / NCIMB 1071
J. Gen. Appl. Microbiol.
49
51-58
2003
-
-
-
-
-
-
-
-
2
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
656314
Isobe
Crystallization and some prope ...
Staphylococcus sp., Staphylococcus sp. LDH-1
J. Biosci. Bioeng.
94
330-335
2002
-
-
-
-
-
-
3
4
-
-
2
-
-
3
-
-
1
-
-
-
1
-
11
2
1
1
-
-
2
-
1
2
-
1
-
-
-
-
2
-
-
-
-
3
-
4
-
-
2
-
-
-
-
1
-
-
1
-
11
2
1
1
-
-
2
-
1
1
-
-
-
-
-
-
656500
Razeto
Domain closure, substrate spec ...
Lactobacillus delbrueckii subsp. bulgaricus
J. Mol. Biol.
318
109-119
2002
-
-
-
1
1
-
-
-
-
-
-
-
-
3
-
-
-
1
-
-
-
-
2
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
2
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
286501
Kochhar
Roles of His205, His296, His30 ...
Lactobacillus delbrueckii subsp. bulgaricus
Eur. J. Biochem.
267
1633-1639
2000
-
-
-
-
4
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286502
Dym
The crystal structure of D-lac ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
97
9413-9418
2000
-
-
-
1
-
-
-
-
2
-
-
1
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
1
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286500
Stoll
A thioredoxin fusion protein o ...
Enterococcus faecium
Protein Sci.
7
1147-1155
1998
3
-
1
1
-
-
-
3
-
-
-
1
-
3
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
3
-
1
2
1
-
-
-
-
-
3
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286499
Dartois
Purification, properties and D ...
Leuconostoc mesenteroides subsp. cremoris
Res. Microbiol.
146
291-302
1995
-
-
1
-
-
-
-
4
-
-
1
1
-
4
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
4
-
-
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286503
Nessler
Crystallization of D-lactate d ...
Lactobacillus delbrueckii subsp. bulgaricus
J. Mol. Biol.
235
370-371
1994
-
-
-
1
-
-
-
-
-
-
-
1
-
2
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286498
Erwin
Oxidation of D-lactate and L-l ...
Neisseria meningitidis
J. Bacteriol.
175
6382-6391
1993
-
-
1
-
-
-
9
1
1
2
1
1
-
3
-
-
1
-
-
-
-
-
1
-
-
-
-
-
1
-
-
2
-
-
-
-
-
1
2
-
-
-
-
9
-
1
1
2
1
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
286496
Kochhar
Primary structure, physicochem ...
Lactobacillus delbrueckii subsp. bulgaricus
J. Biol. Chem.
267
8499-8513
1992
-
-
-
-
-
-
-
-
-
-
1
1
-
2
-
-
1
-
-
-
-
-
1
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-
-
1
-
-
-
-
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-
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286497
Kochhar
Cloning and overexpression of ...
Lactobacillus delbrueckii subsp. bulgaricus
Biochem. Biophys. Res. Commun.
185
705-712
1992
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1
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2
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5
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1
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286504
Kochhar
Glutamate 264 modulates the pH ...
Lactobacillus delbrueckii subsp. bulgaricus
J. Biol. Chem.
267
20298-20301
1992
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1
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1
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4
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3
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4
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1
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659546
Schmidt
Optimization of a process for ...
Staphylococcus epidermidis
J. Biotechnol.
24
315-327
1992
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1
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1
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1
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1
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286495
Le Bras
Properties of D-lactate dehydr ...
Lactobacillus delbrueckii subsp. bulgaricus
FEMS Microbiol. Lett.
79
89-93
1991
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2
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1
1
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286483
Jaenicke
-
Dimeric lactic dehydrogenase f ...
Cerastoderma edule
Naturwissenschaften
68
205-206
1981
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2
1
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1
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286430
Garvie
Bacterial lactate dehydrogenas ...
Escherichia coli, Eubacterium limosum, Klebsiella aerogenes, Lactobacillus acidophilus, Lactobacillus brevis, Lactobacillus buchneri, Lactobacillus casei, Lactobacillus delbrueckii, Lactobacillus delbrueckii subsp. bulgaricus, Lactobacillus delbrueckii subsp. lactis, Lactobacillus fermentum, Lactobacillus jensenii, Lactobacillus jugurt-helveticus, Lactobacillus leichmannii, Lactobacillus plantarum, Lactobacillus vermiforme, Lactococcus lactis, Leuconostoc lactis, Leuconostoc mesenteroides, Leuconostoc mesenteroides subsp. cremoris, Leuconostoc mesenteroides subsp. dextranicum, Mammalia, Mycoplasma sp., Oenococcus oeni, Pediococcus acidilactici, Pediococcus damnosus, Pediococcus inopinatus, Pediococcus pentosaceus, Selenomonas ruminantium, Staphylococcus aureus, Staphylococcus haemolyticus, Staphylococcus hominis, Staphylococcus sp., Staphylococcus warneri, Weissella confusa, Weissella paramesenteroides, Weissella viridescens
Microbiol. Rev.
44
106-139
1980
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197
11
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37
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37
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37
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15
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8
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74
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74
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197
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11
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37
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37
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15
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8
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286489
Long
-
Comparative enzymology and phy ...
Haliotis cracherodii, Helix aspersa
J. Exp. Zool.
207
237-248
1979
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2
10
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2
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4
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286488
Storey
Lactate dehydrogenase in tissu ...
Helix aspersa
Comp. Biochem. Physiol. B
56
181-187
1977
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1
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286484
LeJohn
D(-)-lactate dehydrogenase fro ...
Phytophthora undulata, Pythium debaryanum, Sapromyces elongatus
Methods Enzymol.
41B
293-298
1975
3
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3
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6
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6
3
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286490
Wittenberger
D(-)-Lactate dehydrogenase fro ...
Eubacterium limosum
Methods Enzymol.
41B
299-303
1975
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1
4
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1
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286491
Long
D-Lactate dehydrogenase from t ...
Limulus polyphemus
Methods Enzymol.
41B
313-323
1975
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1
4
4
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1
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286492
Long
Diphosphopyridine nucleotide-l ...
Alitta virens, Limulus polyphemus
Arch. Biochem. Biophys.
154
696-710
1973
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1
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286493
Purohit
D(-)-lactate dehydrogenase fro ...
Allomyces sp.
Arch. Mikrobiol.
84
287-300
1972
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2
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1
1
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286485
Garland
Salt-induced alteration of D(- ...
Heterostelium pallidum
Biochem. Biophys. Res. Commun.
26
679-685
1967
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286486
Wolin
Fructose-1,6-diphosphate requi ...
Streptococcus equinus
Science
146
775-776
1964
1
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286487
Pascal
-
Sur la configuration du lactat ...
Klebsiella aerogenes
Ann. Inst. Pasteur (Paris)
107
55-62
1964
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