Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.2.3 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)

Cloned (Comment) Organism
-
Saccharomyces cerevisiae

Protein Variants

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

KM Value [mM]

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(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

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Storage Stability

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-lactate + 2 ferricytochrome c
-
Saccharomyces cerevisiae pyruvate + 2 ferrocytochrome c + 2 H+
-
?
(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+
-
?
(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
-
?
additional information ferricyanide used as electron acceptor Saccharomyces cerevisiae ?
-
?
additional information electron acceptors other than ferricytochrome c used Saccharomyces cerevisiae ?
-
?

Turnover Number [1/s]

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

Cofactor

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