Literature summary for 1.8.7.2 extracted from

Glauser, D.A.; Bourquin, F.; Manieri, W.; Schurmann, P.
Characterization of ferredoxin:thioredoxin reductase modified by site-directed mutagenesis (2004), J. Biol. Chem., 279, 16662-16669.

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Protein Variants

Protein Variants	Comment	Organism
C57S	active site mutant, inactive. Spectral analysis indicates a reduced Fe-S cluster which can be reduced by dithionite. Stable protein, forms stable covalent heteroduplexes with active-site mutant thioredoxins Trx f C49S or Trx m C40S	Synechocystis sp.
C87A	active site mutant, inactive. Spectral analysis indicates an oxidized Fe-S cluster. Mutants is unable to form stable covalent heteroduplexes with active-site mutant thioredoxins Trx f C49S or Trx m C40S	Synechocystis sp.
H86Y	active site mutant, great reduction in activity. Mutant forms stable covalent heteroduplexes with active-site mutant thioredoxins Trx f C49S or Trx m C40S	Synechocystis sp.

Organism

Organism	UniProt	Comment	Textmining
Synechocystis sp.	-	PCC 6803	-

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Release 2023.1 (January 2023)