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Literature summary for 2.5.1.108 extracted from

  • Dong, M.; Dando, E.; Kotliar, I.; Su, X.; Dzikovski, B.; Freed, J.; Lin, H.
    The asymmetric function of Dph1-Dph2 heterodimer in diphthamide biosynthesis (2019), J. Biol. Inorg. Chem., 24, 777-782 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
C106A the mutant shows wild type activity Saccharomyces cerevisiae
C128A the mutant shows reduced activity compared to the wild type enzyme Saccharomyces cerevisiae
C304A the mutant shows wild type activity Saccharomyces cerevisiae
C362A the mutant shows reduced activity compared to the wild type enzyme Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + L-histidine-[translation elongation factor 2] Saccharomyces cerevisiae
-
S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine-[translation elongation factor 2]
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information no activity is detected using dithionite or the Dph3/Cbr1/NADH system as the reductant Saccharomyces cerevisiae ?
-
-
S-adenosyl-L-methionine + L-histidine-[translation elongation factor 2]
-
Saccharomyces cerevisiae S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine-[translation elongation factor 2]
-
?

Subunits

Subunits Comment Organism
heterodimer 1 * 60000 + 1 * 40000, SDS-PAGE Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
Dph1-Dph2
-
Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
[4Fe-4S]-center
-
Saccharomyces cerevisiae