Literature summary for 4.2.1.22 extracted from

Ereno-Orbea, J.; Majtan, T.; Oyenarte, I.; Kraus, J.P.; Martinez-Cruz, L.A.
Structural insight into the molecular mechanism of allosteric activation of human cystathionine beta-synthase by S-adenosylmethionine (2014), Proc. Natl. Acad. Sci. USA, 111, E3845-E3852 .

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Activating Compound

Activating Compound	Comment	Organism	Structure
S-adenosyl-L-methionine	allosteric activator, in the presence of AdoMet, the autoinhibition exerted by the regulatory region is eliminated	Homo sapiens

Cloned(Commentary)

Cloned (Comment)	Organism
-	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of CBS with bound AdoMet. Binding of AdoMet triggers a conformational change in the Bateman module of the regulatory domain that favors its association with a Bateman module of the complementary subunit to form an antiparallel CBS module. In the presence of AdoMet, the autoinhibition exerted by the regulatory region is eliminated	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P35520	-	-

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Release 2023.1 (January 2023)