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Literature summary for 2.7.7.50 extracted from

  • Chu, C.; Das, K.; Tyminski, J.R.; Bauman, J.D.; Guan, R.; Qiu, W.; Montelione, G.T.; Arnold, E.; Shatkin, A.J.
    Structure of the guanylyltransferase domain of human mRNA capping enzyme (2011), Proc. Natl. Acad. Sci. USA, 108, 10104-10108.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of residues 229-567, comprising the minimum enzymatically active human guanylyltransferase domain, to 3.0 A Homo sapiens

Protein Variants

Protein Variants Comment Organism
D532A inactive Homo sapiens
E234A mutation does not inhibit the formation of the phosphoamide intermediate Homo sapiens
K458A inactive Homo sapiens
K460A inactive Homo sapiens
K533A inactive Homo sapiens
additional information residues 229–567 comprise the minimum enzymatically active human guanylyltransferase domain Homo sapiens
R528A poor activity Homo sapiens
R530A inactive Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens O60942
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