EC number:4.4.1.1

Enzyme

Download
EC Tree
     4. Lyases
        4.4 Carbon-sulfur lyases
            4.4.1 Carbon-sulfur lyases (only sub-subclass identified to date)
ID:4.4.1.1
Description:Cystathionine gamma-lyase.
Alternative Name: Homoserine dehydratase.
Homoserine deaminase.
Gamma-cystathionase.
Cystine desulfhydrase.
Cysteine desulfhydrase.
Cystathioninase.
Cystathionase.
Prosite: PDOC00677;
PDB:
PDBScop
Cath: 3.40.640.10; 3.90.1150.10;

3D structure

Click one PDB to see exact 3D structure provided by NGL.

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.
PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 4.4.1.1
BRENDA Enzyme Link: BRENDA 4.4.1.1
KEGG Enzyme Link: KEGG4.4.1.1
BioCyc Enzyme Link: BioCyc 4.4.1.1
ExPASy Enzyme Link: ExPASy4.4.1.1
EC2PDB Enzyme Link: EC2PDB 4.4.1.1
ExplorEnz Enzyme Link: ExplorEnz 4.4.1.1
PRIAM enzyme-specific profiles Link: PRIAM 4.4.1.1
IntEnz Enzyme Link: IntEnz 4.4.1.1
MEDLINE Enzyme Link: MEDLINE 4.4.1.1

EC number:4.4.1.1

MSA:

4.4.1.1;
Phylogenetic Tree:

4.4.1.1;
Uniprot:
M-CSA:
RHEA:24931 H2O + L-cysteine = H(+) + hydrogen sulfide + NH4(+) + pyruvate
RULE(radius=1) [*:1]-[CH;+0:2](-[NH2;+0:3])-[CH2;+0:4]-[SH;+0:5].[OH2;+0:6]>>[*:1]-[C;H0;+0:2](-[CH3;+0:4])=[O;H0;+0:6].[NH3;+0:3].[SH2;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
L-cysteine desulfidase: an [4Fe-4S] enzyme isolated from Methanocaldococcus jannaschii that catalyzes the breakdown of L-cysteine into pyruvate, ammonia, and sulfide.Tchong SI, Xu H, White RH2005 Feb 815683250
RHEA:24923 L-homoserine = 2-oxobutanoate + NH4(+)
RULE(radius=1) [*:1]-[CH;+0:2](-[NH2;+0:3])-[*:4]-[CH2;+0:5]-[OH;+0:6]>>[*:1]-[C;H0;+0:2](=[O;H0;+0:6])-[*:4]-[CH3;+0:5].[NH3;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
PURIFICATION AND PROPERTIES OF THE CYSTATHIONINE GAMMA-CLEAVAGE ENZYME OF NEUROSPORA.FLAVIN M, SEGAL A1964 Jul14209951
A crystalline enzyme that cleaves homoserine and cystathionine. IV. Mechanism of action, reversibility, and substrate specificity.MATSUO Y, GREENBERG DM1959 Mar13641251
A crystalline enzyme that cleaves homoserine and cystathionine. III. Coenzyme resolution, activators, and inhibitors.MATSUO Y, GREENBERG DM1959 Mar13641250
RHEA:14005 H2O + L,L-cystathionine = 2-oxobutanoate + L-cysteine + NH4(+)
RULE(radius=1) [*:1]-[CH;+0:2](-[NH2;+0:3])-[*:4]-[CH2;+0:5]-[S;H0;+0:6]-[*:7].[OH2;+0:8]>>[*:1]-[C;H0;+0:2](=[O;H0;+0:8])-[*:4]-[CH3;+0:5].[*:7]-[SH;+0:6].[NH3;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
An O-acetylserine(thiol)lyase homolog with L-cysteine desulfhydrase activity regulates cysteine homeostasis in Arabidopsis.Alvarez C, Calo L, Romero LC, García I, Gotor C2010 Feb19955263
Structural basis for the inhibition mechanism of human cystathionine gamma-lyase, an enzyme responsible for the production of H(2)S.Sun Q, Collins R, Huang S, Holmberg-Schiavone L, Anand GS, Tan CH, van-den-Berg S, Deng LW, Moore PK, Karlberg T, Sivaraman J2009 Jan 3019019829
H2S as a physiologic vasorelaxant: hypertension in mice with deletion of cystathionine gamma-lyase.Yang G, Wu L, Jiang B, Yang W, Qi J, Cao K, Meng Q, Mustafa AK, Mu W, Zhang S, Snyder SH, Wang R2008 Oct 2418948540
Conversion of methionine to cysteine in Bacillus subtilis and its regulation.Hullo MF, Auger S, Soutourina O, Barzu O, Yvon M, Danchin A, Martin-Verstraete I2007 Jan17056751
Kinetics and inhibition of recombinant human cystathionine gamma-lyase. Toward the rational control of transsulfuration.Steegborn C, Clausen T, Sondermann P, Jacob U, Worbs M, Marinkovic S, Huber R, Wahl MC1999 Apr 3010212249