Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.1.1.50 extracted from

  • Toms, A.V.; Kinsland, C.; McCloskey, D.E.; Pegg, A.E.; Ealick, S.E.
    Evolutionary links as revealed by the structure of Thermotoga maritima S-adenosylmethionine decarboxylase (2004), J. Biol. Chem., 279, 33837-33846.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapour diffusion method, structures of the wild-type proenzyme and the S63A mutant at 1.55 A and 1.7 A resolution Thermotoga maritima

Protein Variants

Protein Variants Comment Organism
C83A mutant proenzyme is cleaved more rapidly than the wild-type enzyme Thermotoga maritima
H68A mutant proenzyme is cleaved much more slowly than the wild-type enzyme Thermotoga maritima
S55A mutant proenzyme is cleaved more rapidly than the wild-type enzyme Thermotoga maritima
S63A the mutation traps the enzyme in the proenzyme form Thermotoga maritima

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Thermotoga maritima critical regulatory enzyme of the polyamine biosynthetic pathway ?
-
?

Organism

Organism UniProt Comment Textmining
Thermotoga maritima
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Thermotoga maritima

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information critical regulatory enzyme of the polyamine biosynthetic pathway Thermotoga maritima ?
-
?