Literature summary 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.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
4.1.1.50	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

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

Natural Substrates/ Products (Substrates)

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

Organism

EC Number	Organism	UniProt	Comment	Textmining
4.1.1.50	Thermotoga maritima	-	-	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
4.1.1.50	-	Thermotoga maritima

Substrates and Products (Substrate)

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

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Release 2023.1 (January 2023)