Literature summary for 4.2.1.22 extracted from

Pey, A.L.; Martinez-Cruz, L.A.; Kraus, J.P.; Majtan, T.
Oligomeric status of human cystathionine beta-synthase modulates AdoMet binding (2016), FEBS Lett., 590, 4461-4471 .

Search for more literature for 4.2.1.22

Cloned(Commentary)

Cloned (Comment)	Organism
-	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
D198V	pathogenic mutation, no impact on specific activity and response to AdoMet	Homo sapiens
D444N	pathogenic mutation, increased basal activity	Homo sapiens
E201S	mutation leads to permanent activation of enzyme	Homo sapiens
additional information	removal of the loop of residues 516-525 functionally eliminates the high affinity sites responsible for kinetic stabilization of the full-length enzyme and yields a dimeric AdoMet-inducible enzyme, in which kinetic stabilization is now exerted by AdoMet binding to the remaining low affinity sites	Homo sapiens
R125Q	pathogenic mutation, no impact on specific activity and response to AdoMet	Homo sapiens
S466L	pathogenic mutation, increased basal activity	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P35520	-	-

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
51.2	-	wild-type, melting temperature, regulatory domains	Homo sapiens
67	-	wild-type, melting temperature, catalytic domains	Homo sapiens

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Release 2023.1 (January 2023)