Information on EC 1.8.3.7 - formylglycine-generating enzyme

for references in articles please use BRENDA:EC1.8.3.7
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.8.3.7
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RECOMMENDED NAME
GeneOntology No.
formylglycine-generating enzyme
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a [sulfatase]-L-cysteine + O2 + 2 a thiol = a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
[sulfatase]-L-cysteine:oxygen oxidoreductase (3-oxo-L-alanine-forming)
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
a [sulfatase]-L-cysteine + O(2) + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
show the reaction diagram
a [sulfatase]-L-cysteine + O2 + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
show the reaction diagram
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 + O2 + hydrogen sulfide + oxidized dithiothreitol
?
show the reaction diagram
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-
-
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?
Ac-Al-3-oxo-L-Ala-TPSRGSLFTGR-NH2 + hydrogen sulfide + oxidized dithiothreitol + H2O
?
show the reaction diagram
acetyl-MTDFYVPVSLCTPSRAALLTGRS-amide + O2 + dithiotreitol
?
show the reaction diagram
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-
-
-
?
acetyl-Tyr-Tyr-Thr-Ser-Pro-Met-3-oxo-Ala-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn-COOH + O2 + dithionite
?
show the reaction diagram
LCSPSRGSLFTGR + O2 + dithiothreitol
leucyl-formylglycyl-SPSRGSLFTGR + ?
show the reaction diagram
LCSPSRGSLFTGR + O2 + dithiothreitol
leucyl-formylglycyl-SPSRGSLFTGR + sulfide + oxidized dithiothreitol + H2O
show the reaction diagram
NH2-Tyr-Tyr-Thr-Ser-Pro-Met-3-oxo-Ala-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn-COOH + O2 + dithionite
?
show the reaction diagram
NH2-Tyr-Tyr-Thr-Ser-Pro-Met-Cys-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn-COOH + O2 + dithionite
?
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
a [sulfatase]-L-cysteine + O(2) + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
show the reaction diagram
a [sulfatase]-L-cysteine + O2 + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
[4Fe-4S]-center
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the enzyme contains three [4Fe-4S] clusters
additional information
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the enzyme is cofactor-independent
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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the enzyme does not require a divalent cation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
Q8NBK9
proprotein convertases like furin, PACE4, and PC5a process and thereby inactivate formylglycine-generating enzyme
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
O2
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for maximal activity the enzyme requires an O2 concentration of 9% (0.105 mM)
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 0.58
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0001 - 0.18
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00011 - 1.833
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Q8NBK9
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Manually annotated by BRENDA team
Q8NBK9
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Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with bromide and iodide ions, using 20-25% (w/v) PEG 4000, 0.1 M Tris-HCl pH 8.0-9.0, 0.2-0.3 M CaCl2
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using 20-25% (w/v) PEG 4000/0.1 M Tris-HCl, pH 8.0-9.0, 0.2-0.3 M CaCl2
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vapor diffusion method, using 100 mM Tris, 2.4 M ammonium formate, 0.3% (w/v) beta-octylglucoside, 3.2% (v/v) 2-butanol, pH 8.0
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in complex with in complex with either Ag+ or Cd2+
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
amylose resin column chromatography
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HisTrap column chromatography
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HisTrap column chromatography and Superdex 200 gel filtration
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HisTrap column chromatography, and Superdex 200 gel filtration
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HisTrap Excel resin column chromatography and Sephadex G-25 gel filtration
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MonoQ column chromatography
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Ni-NTA column chromatography and Sephadex G-25 gel filtration
Ni-NTA column chromatography, Talon metal affinity resin column chromatography, and Sephadex G-25 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in COS-7 cells
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expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Hi5 cells
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expressed in Sf9 cells and High Five cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the expression of endogenous enzyme is particularly low in human brain
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C341S
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active site mutant
C346W
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the mutant show reduced enzyme activity
E130D
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the mutation is associated with multiple sulfatase deficiency
G247R
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the mutant show reduced enzyme activity
G263V
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the mutant show reduced enzyme activity
R364C
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the mutant show reduced enzyme activity
S234R
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the mutant show reduced enzyme activity
C187A
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the mutation leads to an increase of enzyme activity
C187A/C231A/C284S/C298A
C187A/C231A/Y273F/C284S/C298A
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the mutations lead to an increase of enzyme activity
C187A/C284S/C298A
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the mutations lead to an increase of enzyme activity
C274S
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inactive
C296S
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inactive
C298A
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the in vitro activity is not affected by the mutation
S266A
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the mutant shows reduced activity compared to the wild type enzyme
S290K
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the mutant shows very low activity compared to the wild type enzyme
Y273F
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the mutation leads to an increase of enzyme activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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coexpression of formylglycine-generating enzyme is essential for gene therapy of metachromatic leukodystrophy