KEGG   ENZYME: 1.8.2.7
Entry
EC 1.8.2.7                  Enzyme                                 
Name
thiocyanate desulfurase;
TcDH;
thiocyanate dehydrogenase
Class
Oxidoreductases;
Acting on a sulfur group of donors;
With a cytochrome as acceptor
Sysname
thiocyanate:cytochrome c oxidoreductase (cyanate and sulfur-forming)
Reaction(IUBMB)
thiocyanate + 2 ferricytochrome c + H2O = cyanate + sulfur + 2 ferrocytochrome c + 2 H+ [RN:R12631]
Reaction(KEGG)
R12631
Substrate
thiocyanate [CPD:C01755];
ferricytochrome c [CPD:C00125];
H2O [CPD:C00001]
Product
cyanate [CPD:C01417];
sulfur [CPD:C00087];
ferrocytochrome c [CPD:C00126];
H+ [CPD:C00080]
Comment
The enzyme, characterized from the haloalkaliphilic sulfur-oxidizing bacterium Thioalkalivibrio paradoxus, contains three copper ions in its active site. It catalyses the direct conversion of thiocyanate into cyanate and elemental sulfur without involvement of molecular oxygen.
History
EC 1.8.2.7 created 2020
Orthology
K24299  thiocyanate desulfurase
Genes
TIG: THII_0490
TNI: TVNIR_2760
TTI: THITH_13335
TTC: FOKN1_0541
THIC: TspCOW1_21980
TBD: Tbd_0914
SNO: Snov_1008
MSL: Msil_3892
MTUN: MTUNDRAET4_0051.1
MEDK: QEV83_03345
MSC: BN69_2544
MBRY: B1812_06360
MROS: EHO51_17375
SYJ: D082_31920
SYNE: Syn6312_0702
HTH: HTH_1020
HTE: Hydth_1016
 » show all
Reference
1  [PMID:32094184]
  Authors
Tikhonova TV, Sorokin DY, Hagen WR, Khrenova MG, Muyzer G, Rakitina TV, Shabalin IG, Trofimov AA, Tsallagov SI, Popov VO
  Title
Trinuclear copper biocatalytic center forms an active site of thiocyanate dehydrogenase.
  Journal
Proc Natl Acad Sci U S A 117:5280-5290 (2020)
DOI:10.1073/pnas.1922133117
  Sequence
[tti:THITH_13335]
Other DBs
ExplorEnz - The Enzyme Database: 1.8.2.7
IUBMB Enzyme Nomenclature: 1.8.2.7
ExPASy - ENZYME nomenclature database: 1.8.2.7
BRENDA, the Enzyme Database: 1.8.2.7

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Chemical substance (7)   
   KEGG COMPOUND (7)   
Chemical reaction (1)   
   KEGG REACTION (1)   
Gene (27)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (17)   
   KEGG MGENES (9)   
All databases (35)   

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