Literature summary for 1.11.1.1 extracted from

Yeh, J.I.; Du, S.; Tortajada, A.; Paulo, J.; Zhang, S.
Peptergents: peptide detergents that improve stability and functionality of a membrane protein, glycerol-3-phosphate dehydrogenase (2005), Biochemistry, 44, 16912-16919.

Search for more literature for 1.11.1.1

Cloned(Commentary)

Cloned (Comment)	Organism
-	Enterococcus casseliflavus

General Stability

General Stability	Organism
The presence of the peptergents V6K, A6D, and a 40:60 mixture of A6D:A6K all extends the enzymatic half-life to over 3-5 times longer than in its absence.	Enterococcus casseliflavus

Organism

Organism	UniProt	Comment	Textmining
Enterococcus casseliflavus	-	-	-

Oxidation Stability

Oxidation Stability	Organism
Npx is labile, rapidly losing activity under aerobic conditions via spontaneous oxidation of its secondary redox center. The enzyme is oxidized over a period of several weeks at 4 °C or 20°C.	Enterococcus casseliflavus
Npx is labile, rapidly losing activity under aerobic conditions via spontaneous oxidation of its secondary redox center. The enzyme is oxidized over a period of several weeks at 4°C or 20°C.	Enterococcus casseliflavus

Purification (Commentary)

Purification (Comment)	Organism
-	Enterococcus casseliflavus

Reaction

Reaction	Comment	Organism	Reaction ID
NADH + H+ + H2O2 = NAD+ + 2 H2O	catalyzes the two-electron reduction of hydrogen peroxide to water using a cysteine-sulfenic acid as a secondary redox center	Enterococcus casseliflavus	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
NADH + H2O2	-	Enterococcus casseliflavus	NAD+ + H2O	-	?
NADH + H2O2	catalyzes the two-electron reduction of hydrogen peroxide to water using a cysteine-sulfenic acid as a secondary redox center	Enterococcus casseliflavus	NAD+ + H2O	-	?

Synonyms

Synonyms	Comment	Organism
Npx	-	Enterococcus casseliflavus

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Release 2023.1 (January 2023)