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Literature summary for 1.1.98.7 extracted from

  • Grove, T.L.; Ahlum, J.H.;Quin, R.M.; Lanz, N.D.; Radle, M.I.; Krebs, C.; Booker, S.J.
    Further Characterization of Cys-Type and Ser-Type Anaerobic Sulfatase Maturating Enzymes Suggests a Commonality in Mechanism of Catalysis (2013), Biochemistry, 52, 2874-2887.
    View publication on PubMed
Search for more literature for 1.1.98.7

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) Clostridium perfringens

Protein Variants

Protein Variants Comment Organism
C15A/C19A/C22A less stable than wild-type enzyme, loss of one of the three [4Fe-4S]2+ clusters Clostridium perfringens

Metals/Ions

Metals/Ions Comment Organism Structure
[4Fe-4S]2+ cluster three [4Fe-4S]2+ clusters per enzyme molecule Clostridium perfringens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45740
-
 gel filtration Clostridium perfringens

Organism

Organism UniProt Comment Textmining
Clostridium perfringens Q8XMQ3
-
-
Clostridium perfringens type A Q8XMQ3
-
-

Storage Stability

Storage Stability Organism
-80°C, 50 mM potassium HEPES, pH 7.5, 500 mM KCl, 10 mM DTT, and 30% glycerol Clostridium perfringens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 ?
Ac-YYTSPMSAPARSMLLTGN + 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
-
 ?
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
-
 ?
Ac-YYTSPMTAPARSMLLTGN + S-adenosyl-L-methionine a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite Clostridium perfringens type A Ac-YYTSPM-(2S)-2-amino-3-oxobutanoyl-APARSMLLTGN + L-methionine + 5'-deoxyadenosine + sulfur dioxide + H2O
-
 ?
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 ?
-
 ?
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 type A ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1* 45740, deduced form the molecular weight of the enzyme/substrate complex Clostridium perfringens

Synonyms

Synonyms Comment Organism
anaerobic sulfatase-maturating enzyme
-
 Clostridium perfringens
nSMEcpe
-
 Clostridium perfringens

General Information

General Information Comment Organism
metabolism involved in the pathway of sulfatase oxidation Clostridium perfringens