Enzyme

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     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.1 Hydro-lyases
ID:4.2.1.22
Description:Cystathionine beta-synthase.
Alternative Name: Serine sulfhydrase.
Methylcysteine synthase.
Beta-thionase.
Prosite: PDOC00700;
PDB:
PDBScop
Cath: 3.10.580.10; 3.90.1530.20; 3.40.50.1100;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.1.22
BRENDA Enzyme Link: BRENDA 4.2.1.22
KEGG Enzyme Link: KEGG4.2.1.22
BioCyc Enzyme Link: BioCyc 4.2.1.22
ExPASy Enzyme Link: ExPASy4.2.1.22
EC2PDB Enzyme Link: EC2PDB 4.2.1.22
ExplorEnz Enzyme Link: ExplorEnz 4.2.1.22
PRIAM enzyme-specific profiles Link: PRIAM 4.2.1.22
IntEnz Enzyme Link: IntEnz 4.2.1.22
MEDLINE Enzyme Link: MEDLINE 4.2.1.22
MSA:

4.2.1.22;

Phylogenetic Tree:

4.2.1.22;

Uniprot:
M-CSA:
RHEA:10112 L-homocysteine + L-serine = H2O + L,L-cystathionine
RULE(radius=1) [*:1]-[CH2;+0:2]-[OH;+0:3].[*:4]-[SH;+0:5]>>[*:1]-[CH2;+0:2]-[S;H0;+0:5]-[*:4].[OH2;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Cystathionine beta-synthase from human liver: improved purification scheme and additional characterization of the enzyme in crude and pure form.Kraus JP, Rosenberg LE1983 Apr 16838228
Purification, crystallization and preliminary crystallographic analysis of the full-length cystathionine β-synthase from Apis mellifera.Oyenarte I, Majtan T, Ereño J, Corral-Rodríguez MA, Klaudiny J, Majtan J, Kraus JP, Martínez-Cruz LA2012 Nov 123143241
Purification, crystallization and preliminary crystallographic analysis of human cystathionine β-synthase.Oyenarte I, Majtan T, Ereño J, Corral-Rodríguez MA, Kraus JP, Martínez-Cruz LA2012 Nov 123143240
Crystal Structures of Cystathionine β-Synthase from Saccharomyces cerevisiae: One Enzymatic Step at a Time.Tu Y, Kreinbring CA, Hill M, Liu C, Petsko GA, McCune CD, Berkowitz DB, Liu D, Ringe D2018 Jun 529630349