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Literature summary for 1.1.1.38 extracted from

  • Yamaguchi M.; Tokushige, M.; Katsuki, H.
    Studies on regulatory functions of malic enzymes II. Purification and molecular properties of nicotinamide adenine dinucleotide-linked malic enzyme from Escherichia coli (1973), J. Biochem., 73, 169-180.
    View publication on PubMed
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Activating Compound

Activating Compound Comment Organism Structure
L-aspartate
-
 Escherichia coli W

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline 0.025 mM, 70% activity lost after 5 min Escherichia coli W
CoA
-
 Escherichia coli W
Cu2+ 0.025 mM, 70% activity lost after 5 min Escherichia coli W
D-malate competitive inhibition Escherichia coli W
malonate competitive inhibition Escherichia coli W
oxaloacetate 50% inhibition with 0.09 mM Escherichia coli W
p-(chloromercuri)benzoate 0.0025 mM, 80% inhibition within 2 min Escherichia coli W

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.055
-
 NAD+
-
 Escherichia coli W
0.32
-
 Mn2+
-
 Escherichia coli W
0.4
-
 L-malate
-
 Escherichia coli W
2.3
-
 NADP+
-
 Escherichia coli W
5
-
 oxaloacetate
-
 Escherichia coli W

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+
-
 Escherichia coli W
Mg2+
-
 Escherichia coli W
Mn2+
-
 Escherichia coli W
Ni2+ requirement for divalent cation Escherichia coli W
Zn2+ requirement for divalent cation Escherichia coli W

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
198000
-
 low speed sedimentation equilibrium Escherichia coli W
203000
-
 sucrose density gradient centrifugation Escherichia coli W

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-malate + NAD+ Escherichia coli W
-
 CO2 + pyruvate + NADH
-
 ?
Oxaloacetate Escherichia coli W
-
 CO2 + pyruvate
-
 ir

Organism

Organism UniProt Comment Textmining
Escherichia coli W
-
-
-

Oxidation Stability

Oxidation Stability Organism
enzyme is reversibly inhibited by air oxidation, activity is completely restored in 30 min by the addition of 2 mM dithiotreitol Escherichia coli W

Purification (Commentary)

Purification (Comment) Organism
streptomycin, ammonium sulfate, heat treatment, acid treatment, calcium phosphate gel, DEAE-sephadex, hydroxylapatite, Sepharose 6B Escherichia coli W

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
177
-
-
 Escherichia coli W

Storage Stability

Storage Stability Organism
4°C, 50 mM Tris-HCl, pH 7.4, 1 mM EDTA, 10 mM 2-mercaptoethanol, 10 mM MgCl2, 5 mM L-aspartate, 2 months, 10% activity lost Escherichia coli W
4°C, 50 mM Tris-HCl, pH 7.4, 1 mM EDTA, 10 mM 2-mercaptoethanol, 2 months, 15% activity lost Escherichia coli W
4°C, 50 mM Tris-HCl, pH 7.4, 1 month, 90% activity lost Escherichia coli W

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-malate + NAD+
-
 Escherichia coli W CO2 + pyruvate + NADH
-
 ?
(S)-malate + NAD+
-
 Escherichia coli W CO2 + pyruvate + NADH
-
 r
(S)-malate + NADP+
-
 Escherichia coli W CO2 + pyruvate + NADPH
-
 ?
Oxaloacetate
-
 Escherichia coli W CO2 + pyruvate
-
 ir
Oxaloacetate NAD+ inhibits oxaloacetate decarboxylation activity Escherichia coli W CO2 + pyruvate
-
 ir

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 with increasing substrate concentrations pH optimum is shifted towards higher pH values Escherichia coli W

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Escherichia coli W
NADP+ 2% activity Escherichia coli W