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Literature summary extracted from

  • Mitra, B.; Gerlt, J.A.; Babbitt, P.C.; Koo, C.W.; Kenyon, G.L.; Joseph, D.; Petsko, G.A.
    A novel structural basis for membrane association of a protein: construction of a chimeric soluble mutant of (S)-mandelate dehydrogenase from Pseudomonas putida (1993), Biochemistry, 32, 12959-12967.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.99.31 expression in Escherichia coli Pseudomonas putida

Protein Variants

EC Number Protein Variants Comment Organism
1.1.99.31 additional information chimeric mutant of (S)-mandelate dehydrogenase with membrane anchoring loop replaced by a portion of glycolate oxidase from spinach is soluble and retains partial catalytic activity (about 1%) using (S)-mandelate as substrate. The activities of the soluble mutant enzymes (S)-mandelate dehydrogenase with residues 2-4 deleted and (S)-mandelate dehydrogenase with 17 residues deleted at the carboxy terminus are nearly the same when (S)-phenyllactate is used as substrate Pseudomonas putida

General Stability

EC Number General Stability Organism
1.1.99.31 repeated freeze-thaw cycles cause significant loss of activity Pseudomonas putida

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.99.31 0.158
-
 (S)-Mandelate pH 7.5, (S)-mandelate dehydrogenase with 17 residues deleted at the carboxy terminus Pseudomonas putida
1.1.99.31 0.206
-
 (S)-Mandelate pH 7.5, wild-type enzyme Pseudomonas putida
1.1.99.31 0.225
-
 (S)-Mandelate pH 7.5, (S)-mandelate dehydrogenase with residues 2-4 deleted Pseudomonas putida
1.1.99.31 0.229
-
 (S)-Mandelate pH 7.5, chimeric mutant of (S)-mandelate dehydrogenase with membrane anchoring loop replaced by a portion of glycolate oxidase from spinach Pseudomonas putida
1.1.99.31 0.78
-
 (S)-phenyllactate pH 7.5, chimeric mutant of (S)-mandelate dehydrogenase with membrane anchoring loop replaced by a portion of glycolate oxidase from spinach Pseudomonas putida
1.1.99.31 2.6
-
 (S)-phenyllactate pH 7.5, wild-type enzyme Pseudomonas putida

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.99.31 membrane associated, wild-type enzyme Pseudomonas putida 16020
-

Organism

EC Number Organism UniProt Comment Textmining
1.1.99.31 Pseudomonas putida
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.99.31 wild-type and mutant enzymes Pseudomonas putida

Storage Stability

EC Number Storage Stability Organism
1.1.99.31 -70°C, wild-type enzyme can be stored frozen in 20% ethanediol for weeks without loss of activity Pseudomonas putida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.99.31 (S)-mandelate + 2,6-dichlorophenolindophenol
-
 Pseudomonas putida 2-oxo-2-phenylacetate + reduced 2,6-dichlorophenolindophenol
-
 ?
1.1.99.31 (S)-phenyllactate + 2,6-dichlorophenolindophenol
-
 Pseudomonas putida ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.99.31 MDH
-
 Pseudomonas putida

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.99.31 1.6
-
 (S)-Mandelate pH 7.5, chimeric mutant of (S)-mandelate dehydrogenase with membrane anchoring loop replaced by a portion of glycolate oxidase from spinach Pseudomonas putida
1.1.99.31 9
-
 (S)-Mandelate pH 7.5, (S)-mandelate dehydrogenase with residues 2-4 deleted Pseudomonas putida
1.1.99.31 24
-
 (S)-Mandelate pH 7.5, (S)-mandelate dehydrogenase with 17 residues deleted at the carboxy terminus Pseudomonas putida
1.1.99.31 174
-
 (S)-Mandelate pH 7.5, wild-type enzyme Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.99.31 FMN
-
 Pseudomonas putida