ID: | 4.2.1.22 | ||
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Description: | Cystathionine beta-synthase. | ||
Alternative Name: |
Serine sulfhydrase. Methylcysteine synthase. Beta-thionase. | ||
Prosite: | PDOC00700; | ||
PDB: |
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Cath: | 3.10.580.10; 3.90.1530.20; 3.40.50.1100; |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.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 |
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 |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Cystathionine beta-synthase from human liver: improved purification scheme and additional characterization of the enzyme in crude and pure form. | Kraus JP, Rosenberg LE | 1983 Apr 1 | 6838228 |
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 LA | 2012 Nov 1 | 23143241 |
Purification, crystallization and preliminary crystallographic analysis of human cystathionine β-synthase. | Oyenarte I, Majtan T, Ereño J, Corral-Rodríguez MA, Kraus JP, Martínez-Cruz LA | 2012 Nov 1 | 23143240 |
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 D | 2018 Jun 5 | 29630349 |