Enzyme

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     2. Transferases
        2.8 Transferring sulfur-containing groups
            2.8.1 Sulfurtransferases
ID:2.8.1.1
Description:Thiosulfate sulfurtransferase.
Alternative Name: Thiosulfate thiotransferase.
Thiosulfate cyanide transsulfurase.
Rhodanese.
Prosite: PDOC00322;
PDB:
PDBScop
1H4M 8031979; 8031980; 8044357; 8044358;
1H4K 8031979; 8031980; 8044357; 8044358;
1E0C 8031979; 8031980; 8044357; 8044358;
2UZQ 8031978; 8044356; 8031978; 8044356; 8031978; 8044356; 8031978; 8044356; 8031978; 8044356; 8031978; 8044356;
4WH9 8031978; 8044356;
 » show all

Cath: 3.40.250.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.8.1.1
BRENDA Enzyme Link: BRENDA 2.8.1.1
KEGG Enzyme Link: KEGG2.8.1.1
BioCyc Enzyme Link: BioCyc 2.8.1.1
ExPASy Enzyme Link: ExPASy2.8.1.1
EC2PDB Enzyme Link: EC2PDB 2.8.1.1
ExplorEnz Enzyme Link: ExplorEnz 2.8.1.1
PRIAM enzyme-specific profiles Link: PRIAM 2.8.1.1
IntEnz Enzyme Link: IntEnz 2.8.1.1
MEDLINE Enzyme Link: MEDLINE 2.8.1.1
MSA:

2.8.1.1;

Phylogenetic Tree:

2.8.1.1;

Uniprot:
M-CSA:
RHEA:16881 hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate
RULE(radius=1) [*:1]#[CH;+0:2].[*:3]=[S;H0;+0:4](-[*:5])(=[O;H0;+0:6])-[SH;+0:7]>>[*:1]#[C;H0;+0:2]-[SH;+0:7].[*:3]=[S;H0;+0:4](-[*:5])-[OH;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Active site cysteinyl and arginyl residues of rhodanese. A novel formation of disulfide bonds in the active site promoted by phenylglyoxal.Weng L, Heinrikson RL, Westley J1978 Nov 25711738
Characterization of a rhodanese from the cyanogenic bacterium Pseudomonas aeruginosa.Cipollone R, Bigotti MG, Frangipani E, Ascenzi P, Visca P2004 Dec 315522204
Identification and characterization of single-domain thiosulfate sulfurtransferases from Arabidopsis thaliana.Bauer M, Papenbrock J2002 Dec 1812482606
PspE (phage-shock protein E) of Escherichia coli is a rhodanese.Adams H, Teertstra W, Koster M, Tommassen J2002 May 811997041
Plant mercaptopyruvate sulfurtransferases: molecular cloning, subcellular localization and enzymatic activities.Nakamura T, Yamaguchi Y, Sano H2000 Sep10951223