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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-AL-3-oxo-L-Ala-TPSRGSLFTGR-NH2 + hydrogen sulfide + oxidized dithiothreitol + H2O
?
Ac-EQSCTAGRAAFITGQGLCTPSRAG-NH2 + O2 + a thiol
?
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-MTDFYVPVSLCTPSRAALLTGRS-amide + O2 + 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 + ?
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
-
-
-
-
?
additional information
?
-
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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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
Elosulfase alfa.
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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0.00012 - 0.0233
Abz-ATTPLCGPSRASILSGR
-
0.0001 - 0.18
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
0.001 - 0.07
Abz-SALCSPTRA-NH2
0.00012
Abz-ATTPLCGPSRASILSGR
pH 8.0, 25°C, mutant enzyme W228F
-
0.00042
Abz-ATTPLCGPSRASILSGR
pH 8.0, 25°C, mutant enzyme S266A
-
0.0233
Abz-ATTPLCGPSRASILSGR
pH 8.0, 25°C, wild-type enzyme
-
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
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0.000317 - 0.045
Abz-ATTPLCGPSRASILSGR
-
0.00011 - 1.833
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
0.0101 - 333.3
Abz-SALCSPTRA-NH2
0.000317
Abz-ATTPLCGPSRASILSGR
pH 8.0, 25°C, mutant enzyme W228F
-
0.00082
Abz-ATTPLCGPSRASILSGR
pH 8.0, 25°C, mutant enzyme S266A
-
0.045
Abz-ATTPLCGPSRASILSGR
pH 8.0, 25°C, wild-type enzyme
-
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
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C346W
the mutant show reduced enzyme activity
G247R
the mutant show reduced enzyme activity
G263V
the mutant show reduced enzyme activity
R364C
the mutant show reduced enzyme activity
S234R
the mutant show reduced enzyme activity
C187A
-
the mutation leads to an increase of enzyme activity
C187A/C231A/Y273F/C284S/C298A
-
the mutations lead to an increase of enzyme activity
C187A/C284S/C298A
-
the mutations lead to an increase of enzyme activity
C298A
-
the in vitro activity is not affected by the mutation
W228F
kcat/Km of the mutant enzyme is fold lower than the wild-type value
Y273F
-
the mutation leads to an increase of enzyme activity
S266A
-
kcat/Km of the mutant enzyme is fold lower than the wild-type value
-
W228F
-
kcat/Km of the mutant enzyme is fold lower than the wild-type value
-
C187A/C231A/C284S/C298A
-
ten-fold increased activity compared to wild-type
-
A177P
the mutant show reduced enzyme activity
A177P
the mutant shows 0.6% of wild type activity
A177P
-
the mutation is associated with multiple sulfatase deficiency
A279V
the mutant show reduced enzyme activity
A279V
the mutant shows 22.9% of wild type activity
A279V
-
the mutation is associated with multiple sulfatase deficiency
A348P
the mutant show reduced enzyme activity
A348P
-
the mutation is associated with multiple sulfatase deficiency
C218Y
the mutant show reduced enzyme activity
C218Y
-
the mutation is associated with multiple sulfatase deficiency
C336R
the mutant show reduced enzyme activity
C336R
-
the mutation is associated with multiple sulfatase deficiency
C336S
inactive
E130D
-
the mutation is associated with multiple sulfatase deficiency
E130D
the mutation is associated with multiple sulfatase deficiency
N259I
the mutant show reduced enzyme activity
N259I
-
the mutation is associated with multiple sulfatase deficiency
P266L
the mutant show reduced enzyme activity
P266L
-
the mutation is associated with multiple sulfatase deficiency
R224W
the mutant show reduced enzyme activity
R224W
-
the mutation is associated with multiple sulfatase deficiency
R345C
the mutant show reduced enzyme activity
R345C
-
the mutation is associated with multiple sulfatase deficiency
R349Q
the mutant show reduced enzyme activity
R349Q
-
the mutation is associated with multiple sulfatase deficiency
R349W
the mutant show reduced enzyme activity
R349W
the mutant shows 0.5% of wild type activity
R349W
-
the mutation is associated with multiple sulfatase deficiency
S155P
the mutant show reduced enzyme activity
S155P
-
the mutation is associated with multiple sulfatase deficiency
W179S
the mutant show reduced enzyme activity
W179S
the mutant shows 2.7% of wild type activity
W179S
-
the mutation is associated with multiple sulfatase deficiency
C263S
-
inactive
C187A/C231A/C284S/C298A
increased activity
C187A/C231A/C284S/C298A
-
the mutant shows increased activity compared to the wild type enzyme
C187A/C231A/C284S/C298A
-
ten-fold increased activity compared to wild-type
C187A/C231A/C284S/C298A
-
the mutations lead to an increase of enzyme activity
C274S
-
inactive
S266A
reduced activity
S266A
-
the mutant shows reduced activity compared to the wild type enzyme
S266A
kcat/Km of the mutant enzyme is fold lower than the wild-type value
S290K
reduced activity
S290K
-
the mutant shows very low activity compared to the wild type enzyme
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Dierks, T.; Schmidt, B.; Borissenko, L.V; Peng, J.; Preusser, A.; Mariappan, M.; von Figura, K.
Multiple sulfatase deficiency is caused by mutations in the gene encoding the human C(alpha)-formylglycine generating enzyme
Cell
113
435-44
2003
Bos taurus
brenda
Dierks, T.; Schmidt, B.; Borissenko, L.V; Peng, J.; Preusser, A.; Mariappan, M.; von Figura, K.
Multiple sulfatase deficiency is caused by mutations in the gene encoding the human C(alpha)-formylglycine generating enzyme
Cell
113
435-444
2003
Homo sapiens (Q8NBK3)
brenda
Dierks, T.; Dickmanns, A.; Preusser-Kunze, A.; Schmidt, B.; Mariappan. M.; von Figura, K.; Ficner, R.; Rudolph, M.G.
Molecular Basis or Multiple Sulfatase Deficiency and Mechanism for Formylglycine Generation of the Human Formylglycine-Generating Enzyme
Cell
121
541-552
2005
Homo sapiens (Q8NBK3), Homo sapiens
brenda
Knop, M.; Engi, P.; Lemnaru, R.; Seebeck, F.P.
In Vitro Reconstitution of Formylglycine-Generating Enzymes Requires Copper(I)
ChemBioChem
16
2147-2150
2015
Mycolicibacterium smegmatis, Thermomonospora curvata, Mycolicibacterium smegmatis DSM 43465, Thermomonospora curvata DSM 43183
brenda
Knop M.; Dang, T.Q.; Jeschke, G.; Seebeck, F.P.
Copper is a Cofactor of the Formylglycine-Generating Enzyme
ChemBioChem
18
161-165
2017
Thermomonospora curvata (Q9F3C7)
brenda
Carlson, B.L.; Ballister, E.R.; Skordalakes, E.; King, D.S.; Breidenbac,h M.A.; Gilmore, S.A.; Berger, J.M.; Bertozzi, C.R.
Function and structure of a prokaryotic formylglycine-generating enzyme
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2008
Mycobacterium tuberculosis (I6Y8I5), Mycobacterium tuberculosis, Streptomyces coelicolor (Q9F3C7), Streptomyces coelicolor, Mycobacterium tuberculosis H37Rv (I6Y8I5), Streptomyces coelicolor M145 (Q9F3C7)
brenda
Fey, J.; Balleininger, M.; Borissenko, L.V.; Schmidt, B.; von Figura, K.; Dierks, T.
Characterization of posttranslational formylglycine formation by luminal components of the endoplasmic reticulum
J. Biol.Chem.
276
47021-47028
2001
Bos taurus
brenda
Roeser, D.; Schmidt, B.; Preusser-Kunze, A.; Rudolph, M.G.
Probing the oxygen-binding site of the human formylglycine-generating enzyme using halide ions
Acta Crystallogr. Sect. D
63
621-627
2007
Homo sapiens (Q8NBK3), Homo sapiens
brenda
Meury, M.; Knop, M.; Seebeck, F.P.
Structural basis for copper-oxygen mediated C-H bond activation by the formylglycine-generating enzyme
Angew. Chem. Int. Ed. Engl.
56
8115-8119
2017
Thermomonospora curvata
brenda
Grove, T.L.; Lee, K.H.; St Clair, J.; Krebs, C.; Booker, S.J.
In vitro characterization of AtsB, a radical SAM formylglycine-generating enzyme that contains three [4Fe-4S] clusters
Biochemistry
47
7523-7538
2008
Klebsiella pneumoniae, Klebsiella pneumoniae ATCC 700721D
brenda
Dierks, T.; Dickmanns, A.; Preusser-Kunze, A.; Schmidt, B.; Mariappan, M.; von Figura, K.; Ficner, R.; Rudolph, M.G.
Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme
Cell
121
541-552
2005
Homo sapiens (Q8NBK3), Homo sapiens
brenda
Knop, M.; Dang, T.Q.; Jeschke, G.; Seebeck, F.P.
Copper is a cofactor of the formylglycine-generating enzyme
ChemBioChem
18
161-165
2017
Thermomonospora curvata
brenda
Knop, M.; Lemnaru, R.; Seebeck, F.P.
Mutation of conserved residues increases in vitro activity of the formylglycine-generating enzyme
ChemBioChem
18
1755-1761
2017
Thermomonospora curvata
brenda
Bojarova, P.; Williams, S.
Sulfotransferases, sulfatases and formylglycine-generating enzymes a sulfation fascination
Curr. Opin. Chem. Biol.
12
573-581
2008
Homo sapiens
brenda
Schlotawa, L.; Radhakrishnan, K.; Baumgartner, M.; Schmid, R.; Schmidt, B.; Dierks, T.; Gaertner, J.
Rapid degradation of an active formylglycine generating enzyme variant leads to a late infantile severe form of multiple sulfatase deficiency
Eur. J. Hum. Genet.
21
1020-1023
2013
Homo sapiens (Q8NBK3), Homo sapiens
brenda
Gande, S.L.; Mariappan, M.; Schmidt, B.; Pringle, T.H.; von Figura, K.; Dierks, T.
Paralog of the formylglycine-generating enzyme - retention in the endoplasmic reticulum by canonical and noncanonical signals
FEBS J.
275
1118-1130
2008
Homo sapiens (Q8NBK3), Homo sapiens
brenda
Peng, J.; Alam, S.; Radhakrishnan, K.; Mariappan, M.; Rudolph, M.G.; May, C.; Dierks, T.; von Figura, K.; Schmidt, B.
Eukaryotic formylglycine-generating enzyme catalyses a monooxygenase type of reaction
FEBS J.
282
3262-3274
2015
Homo sapiens (Q8NBK3)
brenda
Takakusaki, Y.; Hisayasu, S.; Hirai, Y.; Shimada, T.
Coexpression of formylglycine-generating enzyme is essential for synthesis and secretion of functional arylsulfatase A in a mouse model of metachromatic leukodystrophy
Hum. Gene Ther.
16
929-936
2005
Homo sapiens
brenda
Schlotawa, L.; Steinfeld, R.; von Figura, K.; Dierks, T.; Gaertner, J.
Molecular analysis of SUMF1 mutations stability and residual activity of mutant formylglycine-generating enzyme determine disease severity in multiple sulfatase deficiency
Hum. Mutat.
29
205
2008
Homo sapiens (Q8NBK3)
brenda
Mariappan, M.; Preusser-Kunze, A.; Balleininger, M.; Eiselt, N.; Schmidt, B.; Gande, S.L.; Wenzel, D.; Dierks, T.; von Figura, K.
Expression, localization, structural, and functional characterization of pFGE, the paralog of the Calpha-formylglycine-generating enzyme
J. Biol. Chem.
280
15173-15179
2005
Homo sapiens (Q8NBK3)
brenda
Dickmanns, A.; Schmidt, B.; Rudolph, M.G.; Mariappan, M.; Dierks, T.; von Figura, K.; Ficner, R.
Crystal structure of human pFGE, the paralog of the Calpha-formylglycine-generating enzyme
J. Biol. Chem.
280
15180-15187
2005
Homo sapiens (Q8NBK3), Homo sapiens
brenda
Mariappan, M.; Gande, S.L.; Radhakrishnan, K.; Schmidt, B.; Dierks, T.; von Figura, K.
The non-catalytic N-terminal extension of formylglycine-generating enzyme is required for its biological activity and retention in the endoplasmic reticulum
J. Biol. Chem.
283
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2008
Homo sapiens (Q8NBK3)
brenda
Carlson, B.L.; Ballister, E.R.; Skordalakes, E.; King, D.S.; Breidenbach, M.A.; Gilmore, S.A.; Berger, J.M.; Bertozzi, C.R.
Function and structure of a prokaryotic formylglycine-generating enzyme
J. Biol. Chem.
283
20117-20125
2008
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv, Streptomyces coelicolor, Streptomyces coelicolor ATCC BAA-471
brenda
Mariappan, M.; Radhakrishnan, K.; Dierks, T.; Schmidt, B.; von Figura, K.
ERp44 mediates a thiol-independent retention of formylglycine-generating enzyme in the endoplasmic reticulum
J. Biol. Chem.
283
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2008
Homo sapiens (Q8NBK3)
brenda
Ennemann, E.C.; Radhakrishnan, K.; Mariappan, M.; Wachs, M.; Pringle, T.H.; Schmidt, B.; Dierks, T.
Proprotein convertases process and thereby inactivate formylglycine-generating enzyme
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288
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2013
Homo sapiens (Q8NBK3), Homo sapiens
brenda
Holder, P.G.; Jones, L.C.; Drake, P.M.; Barfield, R.M.; Banas, S.; de Hart, G.W.; Baker, J.; Rabuka, D.
Reconstitution of formylglycine-generating enzyme with copper(II) for aldehyde tag conversion
J. Biol. Chem.
290
15730-15745
2015
Homo sapiens (Q8NBK3), Streptomyces coelicolor (Q9F3C7)
brenda
Meshach Paul, D.; Chadah, T.; Senthilkumar, B.; Sethumadhavan, R.; Rajasekaran, R.
Structural distortions due to missense mutations in human formylglycine-generating enzyme leading to multiple sulfatase deficiency
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36
3575-3585
2017
Homo sapiens
brenda
Roeser, D.; Preusser-Kunze, A.; Schmidt, B.; Gasow, K.; Wittmann, J.G.; Dierks, T.; von Figura, K.; Rudolph, M.G.
A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme
Proc. Natl. Acad. Sci. USA
103
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2006
Homo sapiens (Q8NBK3), Homo sapiens
brenda
Krueger, T.; Weiland, S.; Falck, G.; Gerlach, M.; Boschanski, M.; Alam, S.; Mueller, K.M.; Dierks, T.; Sewald, N.
Two-fold bioorthogonal derivatization by different formylglycine-generating enzymes
Angew. Chem. Int. Ed. Engl.
57
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2018
Mycobacterium tuberculosis
brenda
Boschanski, M.; Krueger, T.; Karsten, L.; Falck, G.; Alam, S.; Gerlach, M.; Mueller, B.; Mueller, K.M.; Sewald, N.; Dierks, T.
Site-specific conjugation strategy for dual antibody-drug conjugates using aerobic formylglycine-generating enzymes
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32
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2021
Mycobacterium tuberculosis, Streptomyces coelicolor, Homo sapiens (Q8NBK3)
brenda
Krueger, T.; Dierks, T.; Sewald, N.
Formylglycine-generating enzymes for site-specific bioconjugation
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400
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2019
Mycobacterium tuberculosis, Homo sapiens (Q8NBK3)
brenda
Miarzlou, D.A.; Leisinger, F.; Joss, D.; Haeussinger, D.; Seebeck, F.P.
Structure of formylglycine-generating enzyme in complex with copper and a substrate reveals an acidic pocket for binding and activation of molecular oxygen
Chem. Sci.
10
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2019
Thermomonospora curvata (D1ADF2), Thermomonospora curvata, Thermomonospora curvata ATCC 19995 (D1ADF2)
brenda
Appel, M.J.; Meier, K.K.; Lafrance-Vanasse, J.; Lim, H.; Tsai, C.L.; Hedman, B.; Hodgson, K.O.; Tainer, J.A.; Solomon, E.I.; Bertozzi, C.R.
Formylglycine-generating enzyme binds substrate directly at a mononuclear Cu(I) center to initiate O2 activation
Proc. Natl. Acad. Sci. USA
116
5370-5375
2019
Streptomyces coelicolor (Q9F3C7), Streptomyces coelicolor ATCC BAA-471 (Q9F3C7)
brenda