Any feedback?
Literature summary extracted from
- Further Characterization of Cys-Type and Ser-Type Anaerobic Sulfatase Maturating Enzymes Suggests a Commonality in Mechanism of Catalysis (2013), Biochemistry, 52, 2874-2887.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.1.98.7 | expressed in Escherichia coli BL21(DE3) | Clostridium perfringens |
| 1.8.98.7 | expressed in Escherichia coli BL21(DE3) | Clostridium perfringens |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.1.98.7 | C15A/C19A/C22A | less stable than wild-type enzyme, loss of one of the three [4Fe-4S]2+ clusters | Clostridium perfringens |
| 1.8.98.7 | C15A/C19A/C22A | less stable than wild-type enzyme, loss of one of the three [4Fe-4S]2+ clusters | Clostridium perfringens |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.98.7 | [4Fe-4S]2+ cluster | three [4Fe-4S]2+ clusters per enzyme molecule | Clostridium perfringens |  |
| 1.8.98.7 | [4Fe-4S]2+ cluster | three [4Fe-4S]2+ clusters per enzyme molecule | Clostridium perfringens | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.1.98.7 | 45740 | - |
gel filtration | Clostridium perfringens |
| 1.8.98.7 | 45740 | - |
gel filtration | Clostridium perfringens |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.1.98.7 | Clostridium perfringens | Q8XMQ3 | - |
- |
| 1.1.98.7 | Clostridium perfringens type A | Q8XMQ3 | - |
- |
| 1.8.98.7 | Clostridium perfringens | Q8XMQ3 | - |
- |
| 1.8.98.7 | Clostridium perfringens type A | Q8XMQ3 | - |
- |
Storage Stability
| EC Number | Storage Stability | Organism |
|---|---|---|
| 1.1.98.7 | -80°C, 50 mM potassium HEPES, pH 7.5, 500 mM KCl, 10 mM DTT, and 30% glycerol | Clostridium perfringens |
| 1.8.98.7 | -80°C, 50 mM potassium HEPES, pH 7.5, 500 mM KCl, 10 mM DTT, and 30% glycerol | Clostridium perfringens |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.98.7 | Ac-YYTSPMSAPARSMLLTGN + S-adenosyl-L-methionine | a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite | Clostridium perfringens | Ac-YYTSPM-3-oxo-L-Ala-APARSMLLTGN + L-methionine + 5'-deoxyadenosine | - |
? | |
| 1.1.98.7 | Ac-YYTSPMTAPARSMLLTGN + S-adenosyl-L-methionine | a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite | Clostridium perfringens | Ac-YYTSPM-(2S)-2-amino-3-oxobutanoyl-APARSMLLTGN + L-methionine + 5'-deoxyadenosine + sulfur dioxide + H2O | - |
? | |
| 1.1.98.7 | additional information | the enzme also perfoms the reaction of the Cys-type anaerobic sulfatase-maturating enzyme, converting a serine residue of sulfatase into a 3-oxo-L-alanine residue. The post-translational modification of sulfatases, i.e. the creation of a 3-oxo-L-alanine (i.e. Calpha-formylglycine) residue from a cysteine or serine is vital for the proper function of sulfatases. No reaction with Ac-YYTSPM(allo)TAPARSMLLTGN | Clostridium perfringens | ? | - |
? | |
| 1.8.98.7 | Ac-YTAVPSCIPSRASILTGM + S-adenosyl-L-methionine + dithionite | a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite | Clostridium perfringens | Ac-YTAVPS-3-oxo-L-Ala-IPSRASILTGM + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen sulfide | - |
? | |
| 1.8.98.7 | Ac-YTAVPSCIPSRASILTGM + S-adenosyl-L-methionine + dithionite | a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite | Clostridium perfringens type A | Ac-YTAVPS-3-oxo-L-Ala-IPSRASILTGM + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen sulfide | - |
? | |
| 1.8.98.7 | Ac-YYTSPMCAPARSMLLTGN + S-adenosyl-L-methionine | a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite | Clostridium perfringens | Ac-YYTSPM-3-oxo-L-Ala-APARSMLLTGN + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen sulfide | - |
? | |
| 1.8.98.7 | Ac-YYTSPMCAPARSMLLTGN + S-adenosyl-L-methionine | a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite | Clostridium perfringens type A | Ac-YYTSPM-3-oxo-L-Ala-APARSMLLTGN + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen sulfide | - |
? | |
| 1.8.98.7 | Ac-YYTSPMSAPARSMLLTGN + S-adenosyl-L-methionine | a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite | Clostridium perfringens | Ac-YYTSPM3-oxo-L-Ala-APARSMLLTGN + L-methionine + 5'-deoxyadenosine | - |
? | |
| 1.8.98.7 | Ac-YYTSPMSAPARSMLLTGN + S-adenosyl-L-methionine | a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite | Clostridium perfringens type A | Ac-YYTSPM3-oxo-L-Ala-APARSMLLTGN + L-methionine + 5'-deoxyadenosine | - |
? | |
| 1.8.98.7 | Ac-YYTSPMSeCAPARSMLLTGN + S-adenosyl-L-methionine | a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite | Clostridium perfringens | Ac-YYTSPM-3-oxo-L-Ala-APARSMLLTGN + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen selenide | - |
? | |
| 1.8.98.7 | Ac-YYTSPMSeCAPARSMLLTGN + S-adenosyl-L-methionine | a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite | Clostridium perfringens type A | Ac-YYTSPM-3-oxo-L-Ala-APARSMLLTGN + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen selenide | - |
? | |
| 1.8.98.7 | Ac-YYTSPMTAPARSMLLTGN + S-adenosyl-L-methionine | a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite | Clostridium perfringens | Ac-YYTSPM-(2S)-2-amino-3-oxobutanoyl-APARSMLLTGN + L-methionine + 5'-deoxyadenosine + sulfur dioxide + H2O | - |
? | |
| 1.8.98.7 | additional information | the enzme also perfoms the reaction of the Ser-type anaerobic sulfatase-maturating enzyme, converting a serine residue of sulfatase into a 3-oxo-L-alanine residue. The post-translational modification of sulfatases, i.e. the creation of a 3-oxo-L-alanine (i.e. Calpha-formylglycine) residue from a cysteine or serine is vital for the proper function of sulfatases. No reaction with Ac-YYTSPM(allo)TAPARSMLLTGN | Clostridium perfringens | ? | - |
? | |
| 1.8.98.7 | additional information | the enzme also perfoms the reaction of the Ser-type anaerobic sulfatase-maturating enzyme, converting a serine residue of sulfatase into a 3-oxo-L-alanine residue. The post-translational modification of sulfatases, i.e. the creation of a 3-oxo-L-alanine (i.e. Calpha-formylglycine) residue from a cysteine or serine is vital for the proper function of sulfatases. No reaction with Ac-YYTSPM(allo)TAPARSMLLTGN | Clostridium perfringens type A | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.1.98.7 | monomer | 1* 45740, deduced form the molecular weight of the enzyme/substrate complex | Clostridium perfringens |
| 1.8.98.7 | monomer | 1* 45740, deduced form the molecular weight of the enzyme/substrate complex | Clostridium perfringens |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.1.98.7 | anaerobic sulfatase-maturating enzyme | - |
Clostridium perfringens |
| 1.1.98.7 | nSMEcpe | - |
Clostridium perfringens |
| 1.8.98.7 | anaerobic sulfatase-maturating enzyme | - |
Clostridium perfringens |
| 1.8.98.7 | nSMEcpe | - |
Clostridium perfringens |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.1.98.7 | metabolism | involved in the pathway of sulfatase oxidation | Clostridium perfringens |
| 1.8.98.7 | metabolism | involved in the pathway of sulfatase oxidation | Clostridium perfringens |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
