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Literature summary for 1.2.1.13 extracted from

  • Sparla, F.; Pupillo, P.; Trost, P.
    The C-terminal extension of glyceraldehyde-3-phosphate dehydrogenase subunit B acts as an autoinhibitory domain regulated by thioredoxins and nicotinamide adenine dinucleotide (2002), J. Biol. Chem., 277, 44946-44952.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C18S mutant of GapB subunit still shows stron redox regulation Spinacia oleracea
C274S mutant of GapB subunit still shows stron redox regulation Spinacia oleracea
C285S mutant of GapB subunit still shows stron redox regulation Spinacia oleracea
C349S mutant of GapB subunit is less redox-sensitive than GapB. Active tetramer, unable to aggregate to higher oligomers in presence of NAD+ Spinacia oleracea
C349S/C358S mutant of GapB subunit is less redox-sensitive than GapB. Active tetramer, unable to aggregate to higher oligomers in presence of NAD+ Spinacia oleracea
c358S mutant of GapB subunit is less redox-sensitive than GapB. Active tetramer, unable to aggregate to higher oligomers in presence of NAD+ Spinacia oleracea

Inhibitors

Inhibitors Comment Organism Structure
NAD+ a regulatory disulfide between Cys359 and Cys358 of the C-terminal extension of GapB does form in presence of oxidized thioredoxin. This covalent modification is required for the NAD+-dependent association into higher oligomers and inhibition of the NADPH-dependent activity Spinacia oleracea
thioredoxin a regulatory disulfide between Cys359 and Cys358 of the C-terminal extension of GapB does form in presence of oxidized thioredoxin. This covalent modification is required for the NAD+-dependent association into higher oligomers and inhibition of the NADPH-dependent activity Spinacia oleracea

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
Spinacia oleracea 9507
-

Organism

Organism UniProt Comment Textmining
Spinacia oleracea
-
-
-

Synonyms

Synonyms Comment Organism
GAPDH
-
Spinacia oleracea