Literature summary for 4.2.1.22 extracted from

Sen, S.; Banerjee, R.
A pathogenic linked mutation in the catalytic core of human cystathionine beta-synthase disrupts allosteric regulation and allows kinetic characterization of a full-length dimer (2007), Biochemistry, 46, 4110-4116.

Search for more literature for 4.2.1.22

Cloned(Commentary)

Cloned (Comment)	Organism
mutant enzymes K102N, P78R and P78R/K102N are expressed in Escherichia coli and purified as glutathione S-transferase fusion proteins using recombinant expression	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
K102N	KM for L-serine is about 2fold higher than wild-type value. KM for L-homocysteine is 2fold higher than wild-type value	Homo sapiens
P78R	KM for L-serine is about 4fold higher than wild-type value. KM for L-homocysteine is comparable to wild-type value	Homo sapiens
P78R/K102N	KM for L-serine is about 2fold higher than wild-type value. Mutant enzyme is insensitive to allosteric regulation and unresponsive to S-adenosyl-L-methionine	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-serine + L-homocysteine	-	Homo sapiens	cystathionine + H2O	-	?

Subunits

Subunits	Comment	Organism
More	mutant enzymes K102N and P78R/K102N behaves like wild-type enzyme by native gel chromatography and exist as a mixture of higher-order quaternary states	Homo sapiens

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Release 2023.1 (January 2023)