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Literature summary for 1.1.99.31 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)

Cloned (Comment) Organism
expression in Escherichia coli Pseudomonas putida

Protein Variants

Protein Variants Comment Organism
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

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.158
-
(S)-Mandelate pH 7.5, (S)-mandelate dehydrogenase with 17 residues deleted at the carboxy terminus Pseudomonas putida
0.206
-
(S)-Mandelate pH 7.5, wild-type enzyme Pseudomonas putida
0.225
-
(S)-Mandelate pH 7.5, (S)-mandelate dehydrogenase with residues 2-4 deleted Pseudomonas putida
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
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
2.6
-
(S)-phenyllactate pH 7.5, wild-type enzyme Pseudomonas putida

Localization

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

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
-
-
-

Purification (Commentary)

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

Storage Stability

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
MDH
-
Pseudomonas putida

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
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
9
-
(S)-Mandelate pH 7.5, (S)-mandelate dehydrogenase with residues 2-4 deleted Pseudomonas putida
24
-
(S)-Mandelate pH 7.5, (S)-mandelate dehydrogenase with 17 residues deleted at the carboxy terminus Pseudomonas putida
174
-
(S)-Mandelate pH 7.5, wild-type enzyme Pseudomonas putida

Cofactor

Cofactor Comment Organism Structure
FMN
-
Pseudomonas putida