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Literature summary for 1.1.1.37 extracted from

  • Eprintsev, A.; Gataullina, M.; Lyashchenko, M.
    Physicochemical and catalytic properties of NAD+-dependent malate dehydrogenase isoforms from maize mesophyll (2016), Appl. Biochem. Microbiol., 52, 366-370.
No PubMed abstract available

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
31600
-
-
Zea mays
31600
-
2 * 31600, SDS-PAGE Zea mays
63300
-
enzyme form 2, gel fitration Zea mays
126600
-
enzyme form 1, gel fitration Zea mays

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-malate + NAD+ Zea mays
-
oxaloacetate + NADH + H+
-
r
oxaloacetate + NADH + H+ Zea mays
-
(S)-malate + NAD+
-
r

Organism

Organism UniProt Comment Textmining
Zea mays
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native tetrameric and dimeric MDH enzyme forms, 46 and 71fold, respectively, from mesophyll of maize leaves to homogeneity by ammonium sulfate fractionation, gel filtration, and anion excange chromatography Zea mays

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Zea mays
-
mesophyll
-
Zea mays
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
640
-
purified native enzyme form 1, malate oxidation, pH 8.0, 25°C Zea mays
990
-
purified native enzyme form 2, malate oxidation, pH 8.0, 25°C Zea mays

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-malate + NAD+
-
Zea mays oxaloacetate + NADH + H+
-
r
additional information the tetrameric MDH enzyme form has a higher affinity for NADH and oxaloacetate, and the dimeric has a higher affinity for NAD+ and malate Zea mays ?
-
?
oxaloacetate + NADH + H+
-
Zea mays (S)-malate + NAD+
-
r

Subunits

Subunits Comment Organism
dimer 2 * 31600, SDS-PAGE Zea mays
tetramer 4 * 31600, SDS-PAGE Zea mays

Synonyms

Synonyms Comment Organism
MDH
-
Zea mays
NAD+-dependent malate dehydrogenase
-
Zea mays

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
both reaction directions, assay at Zea mays

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 8.5 oxaloacetate reduction Zea mays
8.5 9.5 malate oxidation Zea mays

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Zea mays
NADH
-
Zea mays

General Information

General Information Comment Organism
metabolism the enzyme is involved in the Krebs cycle (catabolism), glyoxylate and Hatch-Slack cycles, and malate metabolism, as well as other anabolic processes Zea mays