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Literature summary for 1.1.99.28 extracted from

  • Wiegert, T.; Sahm, H.; Sprenger, G.A.
    The substitution of a single amino acid residue (Ser-116->Asp) alters NADP-containing glucose-fructose oxidoreductase of Zymomonas mobilis into a glucose dehydrogenase with dual coenzyme specificity (1997), J. Biol. Chem., 272, 13126-13133.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
S116D a single site mutation S116D alters the enzyme which in the wild type situation contains NAD(P)+ as nondissociable redox cofactor reacting in a ping-pong type mechanism to a dehydrogenase with dissociable NAD(P)+ as cosubstrate and a sequential reaction type Zymomonas mobilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic parameters of the glucose dehydrogenase reaction catalyzed by mutant enzymes Zymomonas mobilis

Organism

Organism UniProt Comment Textmining
Zymomonas mobilis Q07982
-
-

Purification (Commentary)

Purification (Comment) Organism
mutant enzyme S116D Zymomonas mobilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
kinetic parameters of the glucose dehydrogenase reaction catalyzed by mutant enzymes Zymomonas mobilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose + D-fructose
-
Zymomonas mobilis D-glucono-1,5-lactone + D-sorbitol
-
?

Cofactor

Cofactor Comment Organism Structure
NAD+ a single site mutation S116D alters the enzyme which in the wild type situation contains NAD(P)+ as nondissociable redox cofactor reacting in a ping-pong type mechanism to a dehydrogenase with dissociable NAD(P)+ as cosubstrate and a sequential reaction type Zymomonas mobilis
NADH a single site mutation S116D alters the enzyme which in the wild type situation contains NAD(P)+ as nondissociable redox cofactor reacting in a ping-pong type mechanism to a dehydrogenase with dissociable NAD(P)+ as cosubstrate and a sequential reaction type Zymomonas mobilis
NADP+ a single site mutation S116D alters the enzyme which in the wild type situation contains NAD(P)+ as nondissociable redox cofactor reacting in a ping-pong type mechanism to a dehydrogenase with dissociable NAD(P)+ as cosubstrate and a sequential reaction type Zymomonas mobilis
NADPH a single site mutation S116D alters the enzyme which in the wild type situation contains NAD(P)+ as nondissociable redox cofactor reacting in a ping-pong type mechanism to a dehydrogenase with dissociable NAD(P)+ as cosubstrate and a sequential reaction type Zymomonas mobilis