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Literature summary extracted from

  • Sinclair, R.; Reid, G.A.; Chapman, S.K.
    Re-design of Saccharomyces cerevisiae flavocytochrome b2: introduction of L-mandelate dehydrogenase activity (1998), Biochem. J., 333, 117-120.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.2.3
-
Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
1.1.2.3 A198G turnover reduced to 50% Saccharomyces cerevisiae
1.1.2.3 A198G/L230A double mutant enzyme shows significant activity towards L-mandelate Saccharomyces cerevisiae
1.1.2.3 I326A mutant Saccharomyces cerevisiae
1.1.2.3 L230A mutant Saccharomyces cerevisiae
1.1.2.3 L230G mutant Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.2.3 0.49
-
L-lactate wild type enzyme Saccharomyces cerevisiae
1.1.2.3 38
-
L-lactate A198G/L230G mutant enzyme Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.2.3 Fe2+ bound to enzyme Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.2.3 (S)-lactate + 2 ferricytochrome c Saccharomyces cerevisiae can feed electrons to respiratory chain at the level of cytochrome c pyruvate + 2 ferrocytochrome c + 2 H+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.2.3 Saccharomyces cerevisiae
-
-
-

Storage Stability

EC Number Storage Stability Organism
1.1.2.3 -180°C, long term storage Saccharomyces cerevisiae
1.1.2.3 4°C, precipitate from 70% saturated ammonium sulfate, under nitrogen, stable for several weeks Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.2.3 (S)-lactate + 2 ferricytochrome c
-
Saccharomyces cerevisiae pyruvate + 2 ferrocytochrome c + 2 H+
-
?
1.1.2.3 (S)-lactate + 2 ferricytochrome c can feed electrons to respiratory chain at the level of cytochrome c Saccharomyces cerevisiae pyruvate + 2 ferrocytochrome c + 2 H+
-
?
1.1.2.3 (S)-mandelate + ferricytochrome c traces of activity with wild type enzyme, significant activity with A198G/L230G double mutant Saccharomyces cerevisiae hydroxy(phenyl)acetate + ferrocytochrome c
-
?
1.1.2.3 additional information ferricyanide used as electron acceptor Saccharomyces cerevisiae ?
-
?
1.1.2.3 additional information electron acceptors other than ferricytochrome c used Saccharomyces cerevisiae ?
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.2.3 additional information
-
additional information systematic determination of activity of all mutants with L-mandelate and L-lactate as substrate Saccharomyces cerevisiae
1.1.2.3 0.02
-
L-Mandelate wild type enzyme with ferricyanide as electron acceptor Saccharomyces cerevisiae
1.1.2.3 8.5
-
L-Mandelate A198G/L230G mutant enzyme with ferricyanide as electron acceptor Saccharomyces cerevisiae
1.1.2.3 41
-
L-lactate A198G/L230G mutant enzyme with ferricyanide as electron acceptor Saccharomyces cerevisiae
1.1.2.3 400
-
L-lactate wild type enzyme Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.2.3 additional information ferricyanide used as electron acceptor Saccharomyces cerevisiae
1.1.2.3 additional information electron acceptors other than ferricytochrome c used Saccharomyces cerevisiae