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Literature summary extracted from

  • Tolbert, W.D.; Graham, D.E.; White, R.H.; Ealick, S.E.
    Pyruvoyl-dependent arginine decarboxylase from Methanococcus jannaschii: crystal structures of the self-cleaved and S53A proenzyme forms (2003), Structure, 11, 285-294.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.19 expression in Escherichia coli Methanocaldococcus jannaschii

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.19 crystallization of enzyme labeled with selenomethionine, enzyme-agmatine complex and S53A mutant structure, hanging drop method, determination of structure at 1.4 A, crystals belong to space group P2, with cell dimensions a = 56.77 A, b = 92.99 A, c = 87.23 A, and beta = 94.84° Methanocaldococcus jannaschii

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.19 S53A nonprocessing mutant enzyme Methanocaldococcus jannaschii

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.19 Methanocaldococcus jannaschii Q57764
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
4.1.1.19 proteolytic modification the pyruvoyl group of the enzyme is generated by an autocatalytic internal serinolysis reaction at Ser53 in the proenzyme resulting in two polypeptide chains. Asn47, Ser52, Ser53, Ile54, and Glu109 are proposed to play roles in the self-processing reaction Methanocaldococcus jannaschii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.19 L-arginine
-
Methanocaldococcus jannaschii agmatine + CO2
-
?

Subunits

EC Number Subunits Comment Organism
4.1.1.19 trimer
-
Methanocaldococcus jannaschii

Synonyms

EC Number Synonyms Comment Organism
4.1.1.19 PvlArgDC
-
Methanocaldococcus jannaschii
4.1.1.19 pyruvoyl-dependent arginine decraboxylase
-
Methanocaldococcus jannaschii

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.19 additional information the pyruvoyl group of the enzyme is generated by an autocatalytic internal serinolysis reaction at Ser53 in the proenzyme resulting in two polypeptide chains Methanocaldococcus jannaschii