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Literature summary for 6.3.1.14 extracted from

  • Schaffrath, R.; Stark, M.J.
    Decoding the biosynthesis and function of diphthamide, an enigmatic modification of translation elongation factor 2 (EF2) (2014), Microb. Cell, 1, 203-205 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene DPH6, the gene is identified through mining the DPH1-DPH5 interaction network Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + diphthine-[translation elongation factor 2] + NH3 Saccharomyces cerevisiae
-
AMP + diphosphate + diphthamide-[translation elongation factor 2]
-
?
ATP + diphthine-[translation elongation factor 2] + NH3 Saccharomyces cerevisiae ATCC 204508 / S288c
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AMP + diphosphate + diphthamide-[translation elongation factor 2]
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae Q12429
-
-
Saccharomyces cerevisiae ATCC 204508 / S288c Q12429
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + diphthine-[translation elongation factor 2] + NH3
-
Saccharomyces cerevisiae AMP + diphosphate + diphthamide-[translation elongation factor 2]
-
?
ATP + diphthine-[translation elongation factor 2] + NH3
-
Saccharomyces cerevisiae ATCC 204508 / S288c AMP + diphosphate + diphthamide-[translation elongation factor 2]
-
?

Synonyms

Synonyms Comment Organism
diphthamide synthetase
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Saccharomyces cerevisiae
DPH6
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Saccharomyces cerevisiae
YLR143w
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Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
ATP
-
Saccharomyces cerevisiae

General Information

General Information Comment Organism
malfunction a dph6 deletion strain specifically accumulates the diphthine-modified form of EF2, and shows a failure to complete diphthine amidation resulting in loss of ADP ribosylation acceptor activity of EF2 in the presence of diphtheria toxin in vitro. The amidation defect partially protects against DT in vivo and correlates with resistance to EF2 inactivation and growth inhibition by sordarin, collectively traits typical of bona fide diphthamide synthesis mutants Saccharomyces cerevisiae
metabolism the amidation step of diphthamide biosynthesis in yeast requires DPH6, diphthamide synthesis pathway of budding yeast, overview Saccharomyces cerevisiae
physiological function Dph6 is an ATP-dependent diphthamide synthetase that catalyses the reaction using ammonium as a cofactor. Diphthamide is a highly conserved modification of archaeal and eukaryal translation elongation factor 2. Dph6 is the catalytically relevant amidase in the amidation step of diphthamide synthesis Saccharomyces cerevisiae