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Information on EC 3.13.1.7 - carbonyl sulfide hydrolase
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3.13.1.7 carbonyl sulfide hydrolaseIUBMB 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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Word Map
- 3.13.1.7
-
atmospheric
-
aerosol
- thioparus
- anhydrases
-
ambient
- cs2
-
stratospheric
- thiocyanate
- scn
- ozone
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
COS, COS hydrolase, COSase, CS2 hydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
COS
-
-
ambiguous
-
COS hydrolase
COSase
CS2 hydrolase
COS hydrolase
-
-
-
-
COSase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
carbonyl sulfide + H2O = hydrogen sulfide + CO2
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
carbonyl disulfide + H2O
carbonyl sulfide + CO2
-
-
-
-
?
carbonyl sulfide + H2O
hydrogen sulfide + CO2
-
-
-
-
?
additional information
?
-
-
the enzyme cannot convert CO2 to HCO3-
-
-
?
additional information
?
-
-
the enzyme cannot convert CO2 to HCO3-
-
-
?
additional information
?
-
-
the enzyme cannot convert CO2 to HCO3-
-
-
?
additional information
?
-
-
the enzyme cannot convert CO2 to HCO3-
-
-
?
additional information
?
-
-
the enzyme cannot convert CO2 to HCO3-
-
-
?
additional information
?
-
-
the enzyme cannot convert CO2 to HCO3-
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
carbonyl sulfide + H2O
hydrogen sulfide + CO2
-
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SCN-
70% and 20% residual activity at 0.01 and 0.1 mM, respectively
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexadecamer
homotetramer
octamer
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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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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)
brenda
Smeulders, M.J.; Pol, A.; Venselaar, H.; Barends, T.R.; Hermans, J.; Jetten, M.S.; Op den Camp, H.J.
Bacterial CS2 hydrolases from Acidithiobacillus thiooxidans strains are homologous to the archaeal catenane CS2 hydrolase
J. Bacteriol.
195
4046-4056
2013
Acidithiobacillus thiooxidans, Acidithiobacillus thiooxidans S1p, Acidithiobacillus thiooxidans Sts 4-3, Acidithiobacillus thiooxidans 2Bp, Acidithiobacillus thiooxidans BBW1, Acidithiobacillus thiooxidans G8
brenda
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
brenda
Yu, X.; Lin, Y.; Shen, P.; Zhang, Q.; Gupta, D.
Molecular evidences on transport of thiocyanate into rice seedlings and assimilation by 13 C and 15 N labelling and gene expression analyses
Int. Biodeter. Biodegrad.
139
11-17
2019
Oryza sativa
-
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