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Information on EC 3.13.1.7 - carbonyl sulfide hydrolase and Organism(s) Thiobacillus thioparus and UniProt Accession H1AAP2

for references in articles please use BRENDA:EC3.13.1.7
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EC Tree
     3 Hydrolases
         3.13 Acting on carbon-sulfur bonds
             3.13.1 Acting on carbon-sulfur bonds
                3.13.1.7 carbonyl sulfide hydrolase
IUBMB Comments
The enzyme, characterized from the bacterium Thiobacillus thioparus, catalyses a step in the degradation pathway of thiocyanate. This activity is also catalysed by the archaeal EC 3.13.1.5, carbon disulfide lyase.
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This record set is specific for:
Thiobacillus thioparus
UNIPROT: H1AAP2
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Word Map
The taxonomic range for the selected organisms is: Thiobacillus thioparus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
cosase, cos hydrolase, carbonyl sulfide hydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
COS hydrolase
-
-
-
-
COSase
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
carbonyl sulfide hydrogen-sulfide-lyase (decarboxylating)
The enzyme, characterized from the bacterium Thiobacillus thioparus, catalyses a step in the degradation pathway of thiocyanate. This activity is also catalysed by the archaeal EC 3.13.1.5, carbon disulfide lyase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
carbonyl sulfide + H2O
hydrogen sulfide + CO2
show the reaction diagram
-
-
-
?
carbonyl sulfide + H2O
hydrogen sulfide + CO2
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
carbonyl sulfide + H2O
hydrogen sulfide + CO2
show the reaction diagram
-
-
-
?
carbonyl sulfide + H2O
hydrogen sulfide + CO2
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
contains a zinc ion in its catalytic site
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SCN-
70% and 20% residual activity at 0.01 and 0.1 mM, respectively
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06
carbonyl sulfide
at pH 8.5 and 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
58
carbonyl sulfide
at pH 8.5 and 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
960
carbonyl sulfide
at pH 8.5 and 30°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
COSH_THITI
219
0
23353
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme complexed with SCN-, hanging drop vapor diffusion method, using 1.2 M (NH4)2SO4, 0.2 M NaCl, 30% glycerol, 0.1 M Tris-HCl, pH 8.5
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
column chromatography
glutathione-Sepharose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Rosetta-gami B cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ogawa, T.; Noguchi, K.; Saito, M.; Nagahata, Y.; Kato, H.; Ohtaki, A.; Nakayama, H.; Dohmae, N.; Matsushita, Y.; Odaka, M.; Yohda, M.; Nyunoya, H.; Katayama, Y.
Carbonyl sulfide hydrolase from Thiobacillus thioparus strain THI115 is one of the beta-carbonic anhydrase family enzymes
J. Am. Chem. Soc.
135
3818-3825
2013
Thiobacillus thioparus (H1AAP2), Thiobacillus thioparus, Thiobacillus thioparus THI115 (H1AAP2)
Manually annotated by BRENDA team
Ogawa, T.; Hattori, S.; Kamezaki, K.; Kato, H.; Yoshida, N.; Katayama, Y.
Isotopic fractionation of sulfur in carbonyl sulfide by carbonyl sulfide hydrolase of Thiobacillus thioparus THI115
Microbes Environ.
32
367-375
2017
Thiobacillus thioparus, Thiobacillus thioparus THI115
Manually annotated by BRENDA team