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Literature summary for 2.4.1.255 extracted from

  • Sokol, K.A.; Olszewski, N.E.
    The putative eukaryote-like O-GlcNAc transferase of the cyanobacterium Synechococcus elongatus PCC 7942 hydrolyzes UDP-GlcNAc and is involved in multiple cellular processes (2015), J. Bacteriol., 197, 354-361.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
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 Synechococcus elongatus

Protein Variants

Protein Variants Comment Organism
G350D mutation corresponds to G570D mutation in Arabidopsis thaliana, results in plants with altered hormone responses, does not rescue the settling phenotype of the OGT deletion strain Synechococcus elongatus
H280A mutation in residue corresponding to His residue in the human enzyme predicted to be important in the transfer of GlcNAc to substrates, does not rescue the settling phenotype of the OGT deletion strain Synechococcus elongatus
K445A mutation in residue corresponding to His residue in the human enzyme predicted to be important in the transfer of GlcNAc to substrates, does not rescue the settling phenotype of the OGT deletion strain Synechococcus elongatus

Organism

Organism UniProt Comment Textmining
Synechococcus elongatus Q31S86
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-
Synechococcus elongatus PCC 7942 Q31S86
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme is able to hydrolyze UDP-GlcNAc Synechococcus elongatus ?
-
 ?
additional information enzyme is able to hydrolyze UDP-GlcNAc Synechococcus elongatus PCC 7942 ?
-
 ?

Synonyms

Synonyms Comment Organism
Synpcc7942_0051
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 Synechococcus elongatus

General Information

General Information Comment Organism
physiological function an OGT deletion mutant exhibits several phenotypes. Without agitation, mutant cells aggregate and settle out of the medium. The mutant cells have higher free inorganic phosphate levels, wider thylakoid lumen, and differential accumulation of electron-dense inclusion bodies Synechococcus elongatus