Information on EC 4.4.1.27 - carbon disulfide lyase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria

EC NUMBER
COMMENTARY hide
4.4.1.27
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RECOMMENDED NAME
GeneOntology No.
carbon disulfide lyase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
carbon disulfide + 2 H2O = CO2 + 2 hydrogen sulfide
show the reaction diagram
carbon disulfide + H2O = carbonyl sulfide + hydrogen sulfide
show the reaction diagram
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carbonyl sulfide + H2O = CO2 + hydrogen sulfide
show the reaction diagram
(1b)
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SYSTEMATIC NAME
IUBMB Comments
carbon disulfide-lyase (hydrogen sulfide-producing)
The enzyme contains Zn2+. The hyperthermophilic archaeon Acidianus sp. A1-3 obtains energy by the conversion of carbon disulfide to hydrogen sulfide, with carbonyl sulfide as an intermediate.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
no activity in Acidithiobacillus albertensis strain DSM14366
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-
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Manually annotated by BRENDA team
no activity in Acidithiobacillus ferrooxidans strain DSM14882
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Manually annotated by BRENDA team
no activity in Acidithiobacillus thiooxidans strains DSM504 and DSM14887
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
carbon disulfide + 2 H2O
CO2 + 2 hydrogen sulfide
show the reaction diagram
carbonyl sulfide + H2O
CO2 + H2S
show the reaction diagram
carbonyl sulfide + H2O
CO2 + hydrogen sulfide
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
carbon disulfide + 2 H2O
CO2 + 2 hydrogen sulfide
show the reaction diagram
carbonyl sulfide + H2O
CO2 + H2S
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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inability of the small KCN and CF3SO2NH2 to inhibit CS2 hydrolase
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.046 - 0.193
carbon disulfide
0.014 - 0.074
carbonyl sulfide
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
48 - 952
carbon disulfide
1800
carbonyl sulfide
Acidianus sp.
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pH and temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
249 - 64000
carbon disulfide
10417
11000 - 160000
carbonyl sulfide
12966
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
assay at; assay at; assay at
50
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Acidianus sp. (strain A1-3)
Acidianus sp. (strain A1-3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24000
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x * 24000, in the CS2 hydrolase two octameric rings form a hexadecamer by interlocking at right angles to each other, forming a catenane structure, MALDI-TOF MS
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexadecamer
octamer
additional information
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the enzyme exists in solution as a mixture of unique hexadecameric catenane and octameric ring forms, multi-angle laser light scattering and native mass spectrometric analyses, overview. Four of the sixteen active sites of the catenane can be partially blocked due to the packed perpendicular arrangement of the two interlocked rings
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour diffusion method, crystal structures are determined from heterologously expressed selenomethionine-labelled protein at 2.6 A resolution and native purified protein at 2.4 A resolution
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme by ammonium sulfate precipitation, followed by hydrophobic interaction chromatography, and anion exchange chromatography; native enzyme by ammonium sulfate precipitation, followed by hydrophobic interaction chromatography, and anion exchange chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis; DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CS2 starvation reduces the enzyme activity and H2S production within 24 h, profile overview. The activity can be regained within 4 h after end of starvation
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F77A
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Km-value for carbon disulfide is 1.5fold fold lower than wild-type value, Vmax is 1.4fold higher than wild-type value
F96S
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Km-value for carbon disulfide is similar to wild-type value, Vmax is 2.4fold higher than wild-type value
G199stop
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Km-value for carbon disulfide is 1.5fold fold lower than wild-type value, Vmax is 1.2fold higher than wild-type value
F77A
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Km-value for carbon disulfide is 1.5fold fold lower than wild-type value, Vmax is 1.4fold higher than wild-type value
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F96S
-
Km-value for carbon disulfide is similar to wild-type value, Vmax is 2.4fold higher than wild-type value
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G199stop
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Km-value for carbon disulfide is 1.5fold fold lower than wild-type value, Vmax is 1.2fold higher than wild-type value
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