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Information on EC 1.1.1.38 - malate dehydrogenase (oxaloacetate-decarboxylating) and Organism(s) Escherichia coli and UniProt Accession P26616
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1.1.1.38 malate dehydrogenase (oxaloacetate-decarboxylating)IUBMB Comments
Unlike EC 1.1.1.39, malate dehydrogenase (decarboxylating), this enzyme can also decarboxylate oxaloacetate. cf. EC 1.1.1.40, malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+).
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Word Map
- 1.1.1.38
- glucose-6-phosphate
-
lipogenic
- phosphoenolpyruvate
-
lipogenesis
- isocitrate
- adipose
- citrate
- thyroid
- acetyl-coa
-
carboxykinase
- co2
- 6-phosphogluconate
- cholesterol
- triglyceride
- succinate
- nadp+
-
1.1.1.40
- triiodothyronine
- l-malate
-
tricarboxylic
-
nadp+-dependent
- 6-phosphate
- pentose
-
nadp-malic
- nadp-me
-
atp-citrate
- triacylglycerols
-
pigeon
- fumarate
-
oleaginous
-
nadp-linked
-
anaplerotic
- mesophyll
-
refeeding
- pepck
- phosphoglucomutase
-
refeed
- oxalacetate
- alpha-glycerophosphate
- dikinase
-
nadph-generating
- ascaris
- panicum
-
nadp-isocitrate
-
crassulacean
- circinelloides
- hydrogenosomal
- 5'-deiodinase
-
mortierella
- alpina
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
malic enzyme, nad-me, nad-malic enzyme, m-nad(p)-me, malic enzyme 2, mitochondrial nad(p)+-dependent malic enzyme, mitochondrial nad-malic enzyme, nad+-dependent malic enzyme, mitochondrial nad(p) malic enzyme, malate dehydrogenase (oxaloacetate-decarboxylating), 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
malic enzyme
-
-
-
-
NAD-malic enzyme
-
-
-
-
NAD-ME
-
-
-
-
NAD-specific malic enzyme
-
-
-
-
pyruvic-malic carboxylase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
oxidative decarboxylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
(S)-malate:NAD+ oxidoreductase (oxaloacetate-decarboxylating)
Unlike EC 1.1.1.39, malate dehydrogenase (decarboxylating), this enzyme can also decarboxylate oxaloacetate. cf. EC 1.1.1.40, malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+).
CAS REGISTRY NUMBER
COMMENTARY
9080-52-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
oxaloacetate + NADH
(S)-malate + NAD+
-
divalent metal ions are required
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Mg2+
-
stabilizes two distinct conformational states of the enzyme, which differ in response to various substrate and effector concentrations
Mg2+
-
complex sigmoidal saturation curve of free malate concentration in the presence of 5 mM Mg2+
Mn2+
-
stabilizes two distinct conformational states of the enzyme, which differ in response to various substrate and effector concentrations
Mn2+
-
hyperbolic saturation curve of free malate concentration in the presence of 0.3 mM Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-(5-O-phosphono-beta-D-ribofuranosyl)-4-[2-(trifluoromethyl)phenyl]-1H-1,2,3-triazole
-
4-(2-aminophenyl)-1-(5-O-phosphono-beta-D-ribofuranosyl)-1H-1,2,3-triazole
-
4-(2-fluorophenyl)-1-(5-O-phosphono-beta-D-ribofuranosyl)-1H-1,2,3-triazole
-
4-(2-hydroxyethyl)-1-(5-O-phosphono-beta-D-ribofuranosyl)-1H-1,2,3-triazole
-
4-(2-methylphenyl)-1-(5-O-phosphono-beta-D-ribofuranosyl)-1H-1,2,3-triazole
-
4-(4-fluorophenyl)-1-(5-O-phosphono-beta-D-ribofuranosyl)-1H-1,2,3-triazole
-
4-(4-methoxyphenyl)-1-(5-O-phosphono-beta-D-ribofuranosyl)-1H-1,2,3-triazole
-
4-(naphthalen-1-yl)-1-(5-O-phosphono-beta-D-ribofuranosyl)-1H-1,2,3-triazole
-
N-acetyl-1-(5-O-phosphono-beta-D-ribofuranosyl)-1H-1,2,3-triazol-4-amine
-
N-benzoyl-1-(5-O-phosphono-beta-D-ribofuranosyl)-1H-1,2,3-triazol-4-amine
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
inhibition of decarboxylation activity
N-ethylmaleimide
-
L-malate and tartronate strongly protect the enzyme in the presence of MnCl2 and NAD+, 80% inhibition of decarboxylation activity, 10fold increase in reduction activity
ATP
-
more effective in the presence of Mn2+ than in the presence of Mg2+, 50% inhibition with 1.6 mM Mn2+ and 3.9 mM in the presence of Mg2+ respectively
CoA
-
50% inhibition with 0.75 mM CoA in the presence of Mg2+ and 3.4 mM in the presence of Mn2+
additional information
synthesis and inhibitor potencies of triazole moiety-containing nucleotide analogues, overview. The synthesis involves two key steps, the lipase-mediated selective deacylation of 1-azido-2,3,5-tri-O-acetyl-beta-D-ribofuranoside and the Huisgen 1,3-dipolar cycloaddition between terminal alkynes and the 1-azido ribofuranoside derivative
-
additional information
-
synthesis and inhibitor potencies of triazole moiety-containing nucleotide analogues, overview. The synthesis involves two key steps, the lipase-mediated selective deacylation of 1-azido-2,3,5-tri-O-acetyl-beta-D-ribofuranoside and the Huisgen 1,3-dipolar cycloaddition between terminal alkynes and the 1-azido ribofuranoside derivative
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
-
0.5 mM, 2.7fold increase in oxaloacetate reduction activity
N-ethylmaleimide
-
1 mM, 8.9fold increase in oxaloacetate reduction activity
p-chloromercuribenzoate
-
0.02 mM, 2.5fold increase in oxaloacetate reduction activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.09
NAD+
mutant enzyme L310R/R346A/Q401C, pH and temperature not specified in the publication
0.27
NAD+
wild type enzyme, pH and temperature not specified in the publication
0.76
NAD+
mutant enzyme L310R/R346D/Q401C, pH and temperature not specified in the publication
1.11
NAD+
mutant enzyme L310R/R346Y/Q401C, pH and temperature not specified in the publication
2.31
NAD+
mutant enzyme L310R/R346K/Q401C, pH and temperature not specified in the publication
4.83
NAD+
mutant enzyme L310R/R346F/Q401C, pH and temperature not specified in the publication
5
NAD+
mutant enzyme L310R, pH and temperature not specified in the publication
17.2
NAD+
mutant enzyme L310R/Q401C, pH and temperature not specified in the publication
0.13
nicotinamide cytosine dinucleotide
mutant enzyme L310R/Q401C, pH and temperature not specified in the publication
0.29
nicotinamide cytosine dinucleotide
mutant enzyme L310R/R346Y/Q401C, pH and temperature not specified in the publication
0.44
nicotinamide cytosine dinucleotide
mutant enzyme L310R/R346K/Q401C, pH and temperature not specified in the publication
5
nicotinamide cytosine dinucleotide
mutant enzyme L310R/R346A/Q401C, pH and temperature not specified in the publication
5.32
nicotinamide cytosine dinucleotide
mutant enzyme L310R/R346D/Q401C, pH and temperature not specified in the publication
9.4
nicotinamide cytosine dinucleotide
wild type enzyme, pH and temperature not specified in the publication
10.24
nicotinamide cytosine dinucleotide
mutant enzyme L310R/R346F/Q401C, pH and temperature not specified in the publication
102
nicotinamide cytosine dinucleotide
mutant enzyme L310R, pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
NAD+
mutant enzyme L310R/R346A/Q401C, pH and temperature not specified in the publication
0.02
NAD+
mutant enzyme L310R/R346D/Q401C, pH and temperature not specified in the publication
0.08
NAD+
mutant enzyme L310R/R346F/Q401C, pH and temperature not specified in the publication
0.08
NAD+
mutant enzyme L310R/R346Y/Q401C, pH and temperature not specified in the publication
0.18
NAD+
mutant enzyme L310R/R346K/Q401C, pH and temperature not specified in the publication
0.86
NAD+
mutant enzyme L310R/Q401C, pH and temperature not specified in the publication
5.6
NAD+
mutant enzyme L310R, pH and temperature not specified in the publication
57.3
NAD+
wild type enzyme, pH and temperature not specified in the publication
0.12
nicotinamide cytosine dinucleotide
mutant enzyme L310R/R346D/Q401C, pH and temperature not specified in the publication
0.6
nicotinamide cytosine dinucleotide
mutant enzyme L310R, pH and temperature not specified in the publication
0.64
nicotinamide cytosine dinucleotide
mutant enzyme L310R/R346Y/Q401C, pH and temperature not specified in the publication
1.53
nicotinamide cytosine dinucleotide
mutant enzyme L310R/R346A/Q401C, pH and temperature not specified in the publication
2.69
nicotinamide cytosine dinucleotide
mutant enzyme L310R/Q401C, pH and temperature not specified in the publication
3.38
nicotinamide cytosine dinucleotide
mutant enzyme L310R/R346K/Q401C, pH and temperature not specified in the publication
9.33
nicotinamide cytosine dinucleotide
mutant enzyme L310R/R346F/Q401C, pH and temperature not specified in the publication
26.1
nicotinamide cytosine dinucleotide
wild type enzyme, pH and temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
NAD+
mutant enzyme L310R/R346F/Q401C, pH and temperature not specified in the publication
0.03
NAD+
mutant enzyme L310R/R346D/Q401C, pH and temperature not specified in the publication
0.05
NAD+
mutant enzyme L310R/Q401C, pH and temperature not specified in the publication
0.07
NAD+
mutant enzyme L310R/R346Y/Q401C, pH and temperature not specified in the publication
0.08
NAD+
mutant enzyme L310R/R346K/Q401C, pH and temperature not specified in the publication
0.22
NAD+
mutant enzyme L310R/R346A/Q401C, pH and temperature not specified in the publication
0.9
NAD+
mutant enzyme L310R, pH and temperature not specified in the publication
214.8
NAD+
wild type enzyme, pH and temperature not specified in the publication
0.02
nicotinamide cytosine dinucleotide
mutant enzyme L310R/R346D/Q401C, pH and temperature not specified in the publication
0.31
nicotinamide cytosine dinucleotide
mutant enzyme L310R/R346A/Q401C, pH and temperature not specified in the publication
0.91
nicotinamide cytosine dinucleotide
mutant enzyme L310R/R346F/Q401C, pH and temperature not specified in the publication
2.21
nicotinamide cytosine dinucleotide
mutant enzyme L310R/R346Y/Q401C, pH and temperature not specified in the publication
2.8
nicotinamide cytosine dinucleotide
wild type enzyme, pH and temperature not specified in the publication
7.68
nicotinamide cytosine dinucleotide
mutant enzyme L310R/R346K/Q401C, pH and temperature not specified in the publication
20.69
nicotinamide cytosine dinucleotide
mutant enzyme L310R/Q401C, pH and temperature not specified in the publication
169.9
nicotinamide cytosine dinucleotide
mutant enzyme L310R, pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
enzyme inactivation improves the anaerobic production of four-carbon dicarboxylic acids by recombinant Escherichia coli strains expressing oxaloacetate-forming pyruvate carboxylase
PDB
SCOP
CATH
UNIPROT
ORGANISM
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L310R
the mutant strongly prefers nicotinamide cytosine dinucleotide as cofactor over NAD+
L310R/Q401C
L310R/R346A/Q401C
the mutant prefers nicotinamide cytosine dinucleotide as cofactor over NAD+
L310R/R346D/Q401C
the mutant prefers nicotinamide cytosine dinucleotide as cofactor over NAD+
L310R/R346F/Q401C
the mutant strongly prefers nicotinamide cytosine dinucleotide as cofactor over NAD+
L310R/R346K/Q401C
the mutant strongly prefers nicotinamide cytosine dinucleotide as cofactor over NAD+
L310R/R346Y/Q401C
the mutant strongly prefers nicotinamide cytosine dinucleotide as cofactor over NAD+
L310R/Q401C
the mutant prefers nicotinamide cytosine dinucleotide as cofactor over NAD+
L310R/Q401C
the mutant strongly prefers nicotinamide cytosine dinucleotide as cofactor over NAD+
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cook, R.A.
Distinct metal cofactor-induced conformational states in the NAD-specific malic enzyme of Escherichia coli as revealed by proteolysis studies
Biochim. Biophys. Acta
749
198-203
1983
Escherichia coli
Yamaguchi, M.
Studies on regulatory functions of malic enzymes. IV. Effects of sulfhydryl group modification on the catalytic function of NAD-linked malic enzyme from Escherichia coli
J. Biochem.
86
325-333
1979
Escherichia coli
Milne, J.A.; Cook, R.A.
Role of metal cofactors in enzyme regulation. Differences in the regulatory properties of the Escherichia coli nicotinamide adenine dinucleotide specific malic enzyme depending on whether Mg2+ or Mn2+ serves as divalent cation
Biochemistry
18
3605-3610
1979
Escherichia coli
-
Hou, S.; Liu, W.; Ji, D.; Zhao, Z.K.
Efficient synthesis of triazole moiety-containing nucleotide analogs and their inhibitory effects on a malic enzyme
Bioorg. Med. Chem. Lett.
21
1667-1669
2011
Escherichia coli (P26616), Escherichia coli
Skorokhodova, A.; Gulevich, A.; Debabov, V.
Inactivation of malic enzymes improves the anaerobic production of four-carbon dicarboxylic acids by recombinant Escherichia coli strains expressing pyruvate carboxylase
Appl. Biochem. Microbiol.
54
849-854
2018
Escherichia coli (P26616)
-
EXTERNAL LINKS (specific for EC-Number 1.1.1.38)
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