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Information on EC 1.8.3.7 - formylglycine-generating enzyme
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1.8.3.7 formylglycine-generating enzymeIUBMB Comments
Requires a copper cofactor and Ca2+. The enzyme, which is found in both prokaryotes and eukaryotes, catalyses a modification of a conserved L-cysteine residue in the active site of sulfatases, generating a unique 3-oxo-L-alanine residue that is essential for sulfatase activity. The exact nature of the thiol involved is still not clear - dithiothreitol and cysteamine are the most efficiently used thiols in vitro. Glutathione alo acts in vitro, but it is not known whether it is used in vivo.
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Word Map
- 1.8.3.7
-
sulfatases
-
metachromatic
- mucopolysaccharidosis
- leukodystrophy
-
ichthyosis
-
antibody-drug
-
ultra-rare
- morquio
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
a [sulfatase]-L-cysteine
+
+
2
=
a [sulfatase]-3-oxo-L-alanine
+
+
+
Synonyms
sumf1, formylglycine-generating enzyme, formylglycine generating enzyme, sulfatase-modifying factor 1, fgly-generating enzyme, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AtsB
Calpha-formylglycine-generating enzyme 1
-
-
-
-
FGE
formylglycine generating enzyme
sulfatase-modifying factor 1
SUMF1
FGE
-
sulfatase-modifying factor 1
-
-
-
-
SUMF1
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a [sulfatase]-L-cysteine + O2 + 2 a thiol = a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
[sulfatase]-L-cysteine:oxygen oxidoreductase (3-oxo-L-alanine-forming)
Requires a copper cofactor and Ca2+. The enzyme, which is found in both prokaryotes and eukaryotes, catalyses a modification of a conserved L-cysteine residue in the active site of sulfatases, generating a unique 3-oxo-L-alanine residue that is essential for sulfatase activity. The exact nature of the thiol involved is still not clear - dithiothreitol and cysteamine are the most efficiently used thiols in vitro. Glutathione alo acts in vitro, but it is not known whether it is used in vivo.
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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
a [sulfatase]-L-cysteine + O(2) + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
a [sulfatase]-L-cysteine + O2 + 2 a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
a [sulfatase]-L-cysteine + O2 + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
Abz-ATTPLCGPSRASILSGR + O2 + reduced dithiothreitol
? + hydrogen sulfide + oxidized dithiothreitol + H2O
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 + O2 + hydrogen sulfide + oxidized dithiothreitol
?
-
-
-
-
?
Abz-SALCSPTRA-NH2 + O2 + reduced dithiothreitol
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 + H2O + hydrogen sulfide + oxidized dithiothreitol
Ac-EQSCTAGRAAFITGQGLCTPSRAG-NH2 + O2 + reduced dithiothreitol
? + hydrogen sulfide + oxidized dithiothreitol + H2O
accepts the sequence CTPSR. The human enzyme strictly converts proline-containing aldehyde tags, either in vivo or in vitro, whereas in the presence of copper, the enzyme fom Streptomyces coelicolor and Mycobacterium tuberculosis tolerate proline-to-alanine substitutions in the core motif
-
-
?
Ac-LCSPSRGSLFTGR-NH2 + O2 + reduced dithiothreitol
Ac-L-3-oxo-L-Ala-SPSRGSLFTGR-NH2 + H2O + hydrogen sulfide + oxidized dithiothreitol
AC-MTDFYVPVSLCTPSRAALLTGRS-amide + O2 + reduced dithiothreitol
AC-MTDFYVPVSL-3-oxo-Ala-TPSRAALLTGRS-amide + H2O + hydrogen sulfide + oxidized dithiothreitol
-
-
-
-
?
acetyl-Tyr-Tyr-Thr-Ser-Pro-Met-3-oxo-Ala-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn-COOH + O2 + dithionite
?
LCSPSRGSLFTGR + O2 + dithiothreitol
leucyl-formylglycyl-SPSRGSLFTGR + sulfide + oxidized dithiothreitol + H2O
NH2-Tyr-Tyr-Thr-Ser-Pro-Met-3-oxo-Ala-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn-COOH + O2 + dithionite
?
NH2-Tyr-Tyr-Thr-Ser-Pro-Met-Cys-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn-COOH + O2 + dithionite
?
[arylsulfatase A]-L-cysteine69 + O2 + reduced acceptor
[arylsulfatase A]-Calpha-formylglycine69 + hydrogen sulfide + acceptor
-
-
-
-
?
a [sulfatase]-L-cysteine + O(2) + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
-
-
?
a [sulfatase]-L-cysteine + O(2) + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
-
-
-
?
a [sulfatase]-L-cysteine + O2 + 2 a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
preference of the enzyme for CXPXR-type motifs
-
-
?
a [sulfatase]-L-cysteine + O2 + 2 a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
almost exclusively converts the cysteine within the CTPSR motif
-
-
?
a [sulfatase]-L-cysteine + O2 + 2 a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
preference of the enzyme for CXPXR-type motifs
-
-
?
a [sulfatase]-L-cysteine + O2 + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
-
-
-
?
a [sulfatase]-L-cysteine + O2 + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
-
-
?
a [sulfatase]-L-cysteine + O2 + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
-
-
-
?
a [sulfatase]-L-cysteine + O2 + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
-
-
?
a [sulfatase]-L-cysteine + O2 + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
-
-
-
?
a [sulfatase]-L-cysteine + O2 + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
-
-
?
a [sulfatase]-L-cysteine + O2 + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
-
-
-
?
a [sulfatase]-L-cysteine + O2 + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
-
-
?
a [sulfatase]-L-cysteine + O2 + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
-
-
-
?
a [sulfatase]-L-cysteine + O2 + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
-
-
-
?
a [sulfatase]-L-cysteine + O2 + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
-
-
-
?
Abz-ATTPLCGPSRASILSGR + O2 + reduced dithiothreitol
? + hydrogen sulfide + oxidized dithiothreitol + H2O
-
-
-
?
Abz-ATTPLCGPSRASILSGR + O2 + reduced dithiothreitol
? + hydrogen sulfide + oxidized dithiothreitol + H2O
-
-
-
?
Abz-SALCSPTRA-NH2 + O2 + reduced dithiothreitol
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 + H2O + hydrogen sulfide + oxidized dithiothreitol
-
-
-
?
Abz-SALCSPTRA-NH2 + O2 + reduced dithiothreitol
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 + H2O + hydrogen sulfide + oxidized dithiothreitol
-
-
-
?
Abz-SALCSPTRA-NH2 + O2 + reduced dithiothreitol
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 + H2O + hydrogen sulfide + oxidized dithiothreitol
-
-
-
-
?
Abz-SALCSPTRA-NH2 + O2 + reduced dithiothreitol
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 + H2O + hydrogen sulfide + oxidized dithiothreitol
-
-
-
-
?
Abz-SALCSPTRA-NH2 + O2 + reduced dithiothreitol
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 + H2O + hydrogen sulfide + oxidized dithiothreitol
-
-
-
-
?
Abz-SALCSPTRA-NH2 + O2 + reduced dithiothreitol
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 + H2O + hydrogen sulfide + oxidized dithiothreitol
-
-
-
?
Abz-SALCSPTRA-NH2 + O2 + reduced dithiothreitol
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 + H2O + hydrogen sulfide + oxidized dithiothreitol
-
-
-
-
?
Ac-AL-3-oxo-L-Ala-TPSRGSLFTGR-NH2 + hydrogen sulfide + oxidized dithiothreitol + H2O
?
-
-
-
?
Ac-AL-3-oxo-L-Ala-TPSRGSLFTGR-NH2 + hydrogen sulfide + oxidized dithiothreitol + H2O
?
-
-
-
?
Ac-EQSCTAGRAAFITGQGLCTPSRAG-NH2 + O2 + a thiol
?
-
accepts the sequence CTPSR. The human enzyme strictly convertes proline-containing aldehyde tags, either in vivo or in vitro, whereas in the presence of copper, the enzyme fom Streptomyces coelicolor and Mycobacterium tuberculosis tolerate proline-to-alanine substitutions in the core motif
-
-
?
Ac-EQSCTAGRAAFITGQGLCTPSRAG-NH2 + O2 + a thiol
?
-
accepts the sequence CTPSR. The human enzyme strictly convertes proline-containing aldehyde tags, either in vivo or in vitro, whereas in the presence of copper, the enzyme fom Streptomyces coelicolor and Mycobacterium tuberculosis tolerate proline-to-alanine substitutions in the core motif
-
-
?
Ac-LCSPSRGSLFTGR-NH2 + O2 + reduced dithiothreitol
Ac-L-3-oxo-L-Ala-SPSRGSLFTGR-NH2 + H2O + hydrogen sulfide + oxidized dithiothreitol
-
-
-
?
Ac-LCSPSRGSLFTGR-NH2 + O2 + reduced dithiothreitol
Ac-L-3-oxo-L-Ala-SPSRGSLFTGR-NH2 + H2O + hydrogen sulfide + oxidized dithiothreitol
-
-
-
?
acetyl-Tyr-Tyr-Thr-Ser-Pro-Met-3-oxo-Ala-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn-COOH + O2 + dithionite
?
-
-
-
-
?
acetyl-Tyr-Tyr-Thr-Ser-Pro-Met-3-oxo-Ala-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn-COOH + O2 + dithionite
?
-
-
-
-
?
LCSPSRGSLFTGR + O2 + dithiothreitol
leucyl-formylglycyl-SPSRGSLFTGR + ?
-
-
-
-
?
LCSPSRGSLFTGR + O2 + dithiothreitol
leucyl-formylglycyl-SPSRGSLFTGR + ?
-
-
-
-
?
LCSPSRGSLFTGR + O2 + dithiothreitol
leucyl-formylglycyl-SPSRGSLFTGR + sulfide + oxidized dithiothreitol + H2O
-
-
-
-
?
LCSPSRGSLFTGR + O2 + dithiothreitol
leucyl-formylglycyl-SPSRGSLFTGR + sulfide + oxidized dithiothreitol + H2O
-
-
-
-
?
NH2-Tyr-Tyr-Thr-Ser-Pro-Met-3-oxo-Ala-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn-COOH + O2 + dithionite
?
-
-
-
-
?
NH2-Tyr-Tyr-Thr-Ser-Pro-Met-3-oxo-Ala-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn-COOH + O2 + dithionite
?
-
-
-
-
?
NH2-Tyr-Tyr-Thr-Ser-Pro-Met-Cys-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn-COOH + O2 + dithionite
?
-
-
-
-
?
NH2-Tyr-Tyr-Thr-Ser-Pro-Met-Cys-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn-COOH + O2 + dithionite
?
-
-
-
-
?
additional information
?
-
-
no activity with NH2-Tyr-Tyr-Thr-Ser-Pro-Met-Ala-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn-COOH
-
-
?
additional information
?
-
-
no activity with NH2-Tyr-Tyr-Thr-Ser-Pro-Met-Ala-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn-COOH
-
-
?
additional information
?
-
-
low activity with Abz-SALSSPTRA-NH2
-
-
?
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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
a [sulfatase]-L-cysteine + O(2) + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
a [sulfatase]-L-cysteine + O2 + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
a [sulfatase]-L-cysteine + O(2) + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
-
-
?
a [sulfatase]-L-cysteine + O(2) + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
-
-
-
?
a [sulfatase]-L-cysteine + O2 + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
-
-
-
?
a [sulfatase]-L-cysteine + O2 + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
-
-
?
a [sulfatase]-L-cysteine + O2 + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
-
-
-
?
a [sulfatase]-L-cysteine + O2 + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
-
-
?
a [sulfatase]-L-cysteine + O2 + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
-
-
-
?
a [sulfatase]-L-cysteine + O2 + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
-
-
?
a [sulfatase]-L-cysteine + O2 + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
-
-
-
?
a [sulfatase]-L-cysteine + O2 + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
-
-
?
a [sulfatase]-L-cysteine + O2 + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
-
-
-
?
a [sulfatase]-L-cysteine + O2 + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
-
-
-
?
a [sulfatase]-L-cysteine + O2 + a thiol
a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cu(I)
Cu+
Cu2+
additional information
Cu(I)
the enzyme binds the substrate directly at a mononuclear Cu(I) center to initiate O2 activation. The copper atom is coordinated by two active-site cysteine residues in a nearly linear geometry
Cu(I)
the enzyme (FGE) mediates O2-activation and hydrogen-atom abstraction in an active site that contains Cu(I) coordinated to two cysteine residues. The 1.04 A crystal structure of the enzyme in complex with copper and a cysteine-containing peptide substrate unveils a network of four crystallographic waters and two active site residues that form a highly acidic O2-binding pocket juxtaposed to the trigonal planar tris-cysteine coordinated Cu(I) center
Cu+
copper-metalloenzyme, one equivalent of Cu+ per acive site. No other transition metals can replace copper
Cu2+
the enzyme contains a copper cofactor. The purified enzyme requires preactivation with copper
Cu2+
the enzyme contains a copper cofactor. The purified enzyme requires preactivation with copper
additional information
-
the enzyme does not require a divalent cation
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cu2+
the substrate specificity for the cysteine motifs CTPS is not changed upon addition of the cofactor copper
Cu2+
-
Cu2+-treated enzyme converts both cysteine motifs (CTPSR and CTAGR)
Cu2+
-
Cu2+-treated enzyme converts both cysteine motifs (CTPSR and CTAGR)
additional information
proprotein convertases like furin, PACE4, and PC5a process and thereby inactivate formylglycine-generating enzyme
-
additional information
-
proprotein convertases like furin, PACE4, and PC5a process and thereby inactivate formylglycine-generating enzyme
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
O2
for maximal activity the enzyme requires an O2 concentration of 9% (0.105 mM)
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
arylsulfatase (type i) deficiency
A homozygous missense variant of SUMF1 in the Bedouin population extends the clinical spectrum in ultrarare neonatal multiple sulfatase deficiency.
arylsulfatase (type i) deficiency
A non-conserved miRNA regulates lysosomal function and impacts on a human lysosomal storage disorder.
arylsulfatase (type i) deficiency
A systematic cross-sectional survey of multiple sulfatase deficiency.
arylsulfatase (type i) deficiency
A systematic review and meta-analysis of published cases reveals the natural disease history in multiple sulfatase deficiency.
arylsulfatase (type i) deficiency
Comprehensive clinical, biochemical, radiological and genetic analysis of 28 Turkish cases with suspected metachromatic leukodystrophy and their relatives.
arylsulfatase (type i) deficiency
Expanding the genetic cause of multiple sulfatase deficiency: A novel SUMF1 variant in a patient displaying a severe late infantile form of the disease.
arylsulfatase (type i) deficiency
Long-term disease course of two patients with multiple sulfatase deficiency differs from metachromatic leukodystrophy in a broad cohort.
arylsulfatase (type i) deficiency
Molecular analysis of SUMF1 mutations: stability and residual activity of mutant formylglycine-generating enzyme determine disease severity in multiple sulfatase deficiency.
arylsulfatase (type i) deficiency
Molecular and functional analysis of SUMF1 mutations in multiple sulfatase deficiency.
arylsulfatase (type i) deficiency
Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme.
arylsulfatase (type i) deficiency
Multiple sulfatase deficiency is due to hypomorphic mutations of the SUMF1 gene.
arylsulfatase (type i) deficiency
Multiple Sulfatase Deficiency: A Case Series With a Novel Mutation.
arylsulfatase (type i) deficiency
Multistep, sequential control of the trafficking and function of the multiple sulfatase deficiency gene product, SUMF1 by PDI, ERGIC-53 and ERp44.
arylsulfatase (type i) deficiency
Natural disease history and characterisation of SUMF1 molecular defects in ten unrelated patients with multiple sulfatase deficiency.
arylsulfatase (type i) deficiency
Natural history of multiple sulfatase deficiency: Retrospective phenotyping and functional variant analysis to characterize an ultra-rare disease.
arylsulfatase (type i) deficiency
Neonatal multiple sulfatase deficiency with a novel mutation and review of the literature.
arylsulfatase (type i) deficiency
Rapid degradation of an active formylglycine generating enzyme variant leads to a late infantile severe form of multiple sulfatase deficiency.
arylsulfatase (type i) deficiency
Structural distortions due to missense mutations in human formylglycine-generating enzyme leading to multiple sulfatase deficiency.
arylsulfatase (type i) deficiency
Sulfatase modifying factor 1 trafficking through the cells: from endoplasmic reticulum to the endoplasmic reticulum.
arylsulfatase (type i) deficiency
SUMF1 enhances sulfatase activities in vivo in five sulfatase deficiencies.
arylsulfatase (type i) deficiency
SUMF1 mutations affecting stability and activity of formylglycine generating enzyme predict clinical outcome in multiple sulfatase deficiency.
arylsulfatase (type i) deficiency
Systemic inflammation and neurodegeneration in a mouse model of multiple sulfatase deficiency.
arylsulfatase (type i) deficiency
[Clinical characterization and mutation identification for multiple sulfatase deficiency patients in China].
Breast Neoplasms
Genome-wide expression analysis reveals six contravened targets of EZH2 associated with breast cancer patient survival.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
A homozygous missense variant of SUMF1 in the Bedouin population extends the clinical spectrum in ultrarare neonatal multiple sulfatase deficiency.
Leukodystrophy, Metachromatic
A systematic review and meta-analysis of published cases reveals the natural disease history in multiple sulfatase deficiency.
Leukodystrophy, Metachromatic
AAV1 Mediated Co-expression of Formylglycine-Generating Enzyme and Arylsulfatase A Efficiently Corrects Sulfatide Storage in a Mouse Model of Metachromatic Leukodystrophy.
Leukodystrophy, Metachromatic
Coexpression of Formylglycine-Generating Enzyme Is Essential for Synthesis and Secretion of Functional Arylsulfatase A in a Mouse Model of Metachromatic Leukodystrophy.
Leukodystrophy, Metachromatic
Coexpression of formylglycine-generating enzyme is essential for synthesis and secretion of functional arylsulfatase A in a mouse model of metachromatic leukodystrophy.
Lysosomal Storage Diseases
Long-term disease course of two patients with multiple sulfatase deficiency differs from metachromatic leukodystrophy in a broad cohort.
Mucopolysaccharidoses
A systematic review and meta-analysis of published cases reveals the natural disease history in multiple sulfatase deficiency.
Mucopolysaccharidosis IV
Adeno-associated virus gene transfer in Morquio A disease - effect of promoters and sulfatase-modifying factor 1.
Mucopolysaccharidosis IV
Evaluation of HIV-1 derived lentiviral vectors as transductors of Mucopolysaccharidosis type IV a fibroblasts.
Multiple Sulfatase Deficiency Disease
A homozygous missense variant of SUMF1 in the Bedouin population extends the clinical spectrum in ultrarare neonatal multiple sulfatase deficiency.
Multiple Sulfatase Deficiency Disease
A non-conserved miRNA regulates lysosomal function and impacts on a human lysosomal storage disorder.
Multiple Sulfatase Deficiency Disease
A systematic cross-sectional survey of multiple sulfatase deficiency.
Multiple Sulfatase Deficiency Disease
A systematic review and meta-analysis of published cases reveals the natural disease history in multiple sulfatase deficiency.
Multiple Sulfatase Deficiency Disease
Comprehensive clinical, biochemical, radiological and genetic analysis of 28 Turkish cases with suspected metachromatic leukodystrophy and their relatives.
Multiple Sulfatase Deficiency Disease
Expanding the genetic cause of multiple sulfatase deficiency: A novel SUMF1 variant in a patient displaying a severe late infantile form of the disease.
Multiple Sulfatase Deficiency Disease
Long-term disease course of two patients with multiple sulfatase deficiency differs from metachromatic leukodystrophy in a broad cohort.
Multiple Sulfatase Deficiency Disease
Molecular analysis of SUMF1 mutations: stability and residual activity of mutant formylglycine-generating enzyme determine disease severity in multiple sulfatase deficiency.
Multiple Sulfatase Deficiency Disease
Molecular and functional analysis of SUMF1 mutations in multiple sulfatase deficiency.
Multiple Sulfatase Deficiency Disease
Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme.
Multiple Sulfatase Deficiency Disease
Multiple sulfatase deficiency is due to hypomorphic mutations of the SUMF1 gene.
Multiple Sulfatase Deficiency Disease
Multiple Sulfatase Deficiency: A Case Series With a Novel Mutation.
Multiple Sulfatase Deficiency Disease
Multistep, sequential control of the trafficking and function of the multiple sulfatase deficiency gene product, SUMF1 by PDI, ERGIC-53 and ERp44.
Multiple Sulfatase Deficiency Disease
Natural disease history and characterisation of SUMF1 molecular defects in ten unrelated patients with multiple sulfatase deficiency.
Multiple Sulfatase Deficiency Disease
Natural history of multiple sulfatase deficiency: Retrospective phenotyping and functional variant analysis to characterize an ultra-rare disease.
Multiple Sulfatase Deficiency Disease
Neonatal multiple sulfatase deficiency with a novel mutation and review of the literature.
Multiple Sulfatase Deficiency Disease
Rapid degradation of an active formylglycine generating enzyme variant leads to a late infantile severe form of multiple sulfatase deficiency.
Multiple Sulfatase Deficiency Disease
Structural distortions due to missense mutations in human formylglycine-generating enzyme leading to multiple sulfatase deficiency.
Multiple Sulfatase Deficiency Disease
Sulfatase modifying factor 1 trafficking through the cells: from endoplasmic reticulum to the endoplasmic reticulum.
Multiple Sulfatase Deficiency Disease
SUMF1 mutations affecting stability and activity of formylglycine generating enzyme predict clinical outcome in multiple sulfatase deficiency.
Multiple Sulfatase Deficiency Disease
Systemic inflammation and neurodegeneration in a mouse model of multiple sulfatase deficiency.
Multiple Sulfatase Deficiency Disease
[Clinical characterization and mutation identification for multiple sulfatase deficiency patients in China].
Neoplasms
Genome-wide expression analysis reveals six contravened targets of EZH2 associated with breast cancer patient survival.
Nervous System Diseases
Haplotype structure enables prioritization of common markers and candidate genes in autism spectrum disorder.
Neurodegenerative Diseases
Natural history of multiple sulfatase deficiency: Retrospective phenotyping and functional variant analysis to characterize an ultra-rare disease.
Neuroinflammatory Diseases
Astrocyte dysfunction triggers neurodegeneration in a lysosomal storage disorder.
Neurologic Manifestations
Astrocyte dysfunction triggers neurodegeneration in a lysosomal storage disorder.
Osteoporosis
High-throughput screening of mouse gene knockouts identifies established and novel skeletal phenotypes.
Pulmonary Disease, Chronic Obstructive
Expression, activity and localization of lysosomal sulfatases in Chronic Obstructive Pulmonary Disease.
Pulmonary Disease, Chronic Obstructive
Sulfatase modifying factor 1 (SUMF1) is associated with Chronic Obstructive Pulmonary Disease.
Spinocerebellar Ataxias
Heterozygous deletion of ITPR1, but not SUMF1, in spinocerebellar ataxia type 16.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.39
Abz-ATTPLCGPSRASILSGR
pH 8.0, 25°C, mutant enzyme W228F
-
0.52
Abz-ATTPLCGPSRASILSGR
pH 8.0, 25°C, mutant enzyme S266A
-
0.1
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
-
mutant C187A/C231A/Y273F/C284S/C298A, at pH 8.0 and 25°C
0.21
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
-
mutant C187A/C231A/C284S/C298A, at pH 8.0 and 25°C
0.23
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
-
mutant C187A/C231A/C284S/C298A, at pH 8.0, temperature not specified in the publication
0.28
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
-
mutant C187A/C284S/C298A, at pH 8.0 and 25°C
0.52
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
-
mutant S266A, at pH 8.0, temperature not specified in the publication
0.55
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
-
wild type enzyme, at pH 8.0 and 25°C
0.58
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
-
wild type enzyme, at pH 8.0, temperature not specified in the publication
0.23
Abz-SALCSPTRA-NH2
mutant enzyme C187A/C231A/C284S/C298A, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.005 mM CuSO4, pH 8.0
0.52
Abz-SALCSPTRA-NH2
mutant enzyme S266A, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.005 mM CuSO4, pH 8.0
0.58
Abz-SALCSPTRA-NH2
wild-type enzyme, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.005 mM CuSO4, pH 8.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00012
Abz-ATTPLCGPSRASILSGR
pH 8.0, 25°C, mutant enzyme W228F
-
0.00042
Abz-ATTPLCGPSRASILSGR
pH 8.0, 25°C, mutant enzyme S266A
-
0.0001
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
-
mutant S266A, at pH 8.0, temperature not specified in the publication
0.027
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
-
wild type enzyme, at pH 8.0 and 25°C
0.027
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
-
wild type enzyme, at pH 8.0, temperature not specified in the publication
0.065
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
-
mutant C187A/C284S/C298A, at pH 8.0 and 25°C
0.07
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
-
mutant C187A/C231A/C284S/C298A, at pH 8.0 and 25°C
0.07
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
-
mutant C187A/C231A/C284S/C298A, at pH 8.0, temperature not specified in the publication
0.17
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
-
mutant Y273F, at pH 8.0 and 25°C
0.18
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
-
mutant C187A/C231A/Y273F/C284S/C298A, at pH 8.0 and 25°C
0.001
Abz-SALCSPTRA-NH2
mutant enzyme S266A, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.005 mM CuSO4, pH 8.0
0.01
Abz-SALCSPTRA-NH2
-
mutant enzyme C187A/C231A/C284S/C298A, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, pH 8.0
0.027
Abz-SALCSPTRA-NH2
-
wild-type enzyme, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.002 mM CuSO4, pH 8.0
0.027
Abz-SALCSPTRA-NH2
wild-type enzyme, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.005 mM CuSO4, pH 8.0
0.07
Abz-SALCSPTRA-NH2
-
mutant enzyme C187A/C231A/C284S/C298A, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.002 mM CuSO4, pH 8.0
0.07
Abz-SALCSPTRA-NH2
mutant enzyme C187A/C231A/C284S/C298A, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.005 mM CuSO4, pH 8.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000317
Abz-ATTPLCGPSRASILSGR
pH 8.0, 25°C, mutant enzyme W228F
-
0.00082
Abz-ATTPLCGPSRASILSGR
pH 8.0, 25°C, mutant enzyme S266A
-
0.00011
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
-
mutant S290K, at pH 8.0, temperature not specified in the publication
0.00082
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
-
mutant S266A, at pH 8.0, temperature not specified in the publication
0.048
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
-
wild type enzyme, at pH 8.0, temperature not specified in the publication
0.0483
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
-
wild type enzyme, at pH 8.0 and 25°C
0.233
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
-
mutant C187A/C284S/C298A, at pH 8.0 and 25°C
0.316
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
-
mutant Y273F, at pH 8.0 and 25°C
0.333
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
-
mutant C187A/C231A/C284S/C298A, at pH 8.0 and 25°C
0.333
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
-
mutant C187A/C231A/C284S/C298A, at pH 8.0, temperature not specified in the publication
1.833
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
-
mutant C187A/C231A/Y273F/C284S/C298A, at pH 8.0 and 25°C
0.0101
Abz-SALCSPTRA-NH2
mutant enzyme S290K, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.005 mM CuSO4, pH 8.0
0.333
Abz-SALCSPTRA-NH2
mutant enzyme C187A/C231A/C284S/C298A, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.005 mM CuSO4, pH 8.0
1.7
Abz-SALCSPTRA-NH2
-
wild-type enzyme, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, pH 8.0
8.17
Abz-SALCSPTRA-NH2
mutant enzyme S266A, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.005 mM CuSO4, pH 8.0
17
Abz-SALCSPTRA-NH2
-
mutant enzyme C187A/C231A/C284S/C298A, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, pH 8.0
48.3
Abz-SALCSPTRA-NH2
-
wild-type enzyme, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.002 mM CuSO4, pH 8.0
48.33
Abz-SALCSPTRA-NH2
wild-type enzyme, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.005 mM CuSO4, pH 8.0
333.3
Abz-SALCSPTRA-NH2
-
mutant enzyme C187A/C231A/C284S/C298A, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.002 mM CuSO4, pH 8.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE