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Literature summary for 3.4.24.40 extracted from

  • Massaoud, M.K.; Marokhazi, J.; Venekei, I.
    Enzymatic characterization of a serralysin-like metalloprotease from the entomopathogen bacterium, Xenorhabdus (2011), Biochim. Biophys. Acta, 1814, 1333-1339.
    View publication on PubMed
Search for more literature for 3.4.24.40

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline activity can be restored with the addition of Mn2+, Cu2+ and Co2+ up to 90-200% of its original value, while Zn2+ is inefficient Xenorhabdus kozodoii
EDTA inhibits the activity only partially even either after long incubation or in excess amount Xenorhabdus kozodoii
Zn2+ both the Zn2+ inhibition of protease B activity and its resistance to EDTA inhibition might be caused by an Asp in position 191 where most of the serralysins contain Asn Xenorhabdus kozodoii

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ slightly activating Xenorhabdus kozodoii
Cu2+ slightly activating Xenorhabdus kozodoii

Organism

Organism UniProt Comment Textmining
Xenorhabdus kozodoii
-
-
-
Xenorhabdus kozodoii Morocco
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme by two different steps of anion exchange chromatography Xenorhabdus kozodoii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Boc-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
-
 Xenorhabdus kozodoii ?
-
 ?
Boc-Leu-Ser-Thr-Arg-7-amido-4-methylcoumarin + H2O
-
 Xenorhabdus kozodoii ?
-
 ?
Boc-Leu-Ser-Thr-Arg-7-amido-4-methylcoumarin + H2O
-
 Xenorhabdus kozodoii Morocco ?
-
 ?
Boc-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
-
 Xenorhabdus kozodoii ?
-
 ?
Boc-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
-
 Xenorhabdus kozodoii Morocco ?
-
 ?
Boc-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
-
 Xenorhabdus kozodoii ?
-
 ?
Boc-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
-
 Xenorhabdus kozodoii Morocco ?
-
 ?
D-Ala-Leu-Lys-7-amido-4-methylcoumarin + H2O
-
 Xenorhabdus kozodoii ?
-
 ?
Dabcyl-Glu-Val-Tyr-Ala-Val-Glu-Ser-EDANS + H2O
-
 Xenorhabdus kozodoii ?
-
 ?
DL-Val-Leu-Arg-4-nitroanilide + H2O
-
 Xenorhabdus kozodoii ?
-
 ?
furylacryloyl-Ala-Leu-Val-Tyr + H2O
-
 Xenorhabdus kozodoii ?
-
 ?
furylacryloyl-Leu-Gly-Pro-Ala + H2O
-
 Xenorhabdus kozodoii ?
-
 ?
His-Ser-4-methoxy-2-naphthylamide + H2O
-
 Xenorhabdus kozodoii ?
-
 ?
His-Ser-4-methoxy-2-naphthylamide + H2O
-
 Xenorhabdus kozodoii His-Ser + 4-methoxy-2-naphthylamine
-
 ?
L-Ser-7-amido-4-methylcoumarin + H2O
-
 Xenorhabdus kozodoii L-Ser + 7-amino-4-methylcoumarin
-
 ?
L-Ser-7-amido-4-methylcoumarin + H2O
-
 Xenorhabdus kozodoii Morocco L-Ser + 7-amino-4-methylcoumarin
-
 ?
additional information substrate specificity, and reaction product analysis by electron-spray ionization mass spectrometry, overview. Protease B requires at least three amino acids N-terminal to the scissile bond for detectable hydrolysis. On such substrate protease B is clearly specific for positively charged residues, Arg and Lys, at the P1 substrate position and is rather permissive in the others, but Ser at P1 is preferred in the oligopeptide substrate which contained amino acids also C-terminal to the scissile bond Xenorhabdus kozodoii ?
-
 ?
additional information substrate specificity, and reaction product analysis by electron-spray ionization mass spectrometry, overview. Protease B requires at least three amino acids N-terminal to the scissile bond for detectable hydrolysis. On such substrate protease B is clearly specific for positively charged residues, Arg and Lys, at the P1 substrate position and is rather permissive in the others, but Ser at P1 is preferred in the oligopeptide substrate which contained amino acids also C-terminal to the scissile bond Xenorhabdus kozodoii Morocco ?
-
 ?
N-benzyloxycarbonyl-Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
-
 Xenorhabdus kozodoii ?
-
 ?
Succ-Ala-Ala-Pro-Phe-thiobenzyl ester + H2O
-
 Xenorhabdus kozodoii ?
-
 ?
Succ-Ala-Ala-Pro-Xaa-7-amido-4-methylcoumarin + H2O
-
 Xenorhabdus kozodoii ?
-
 ?

Synonyms

Synonyms Comment Organism
protease B
-
 Xenorhabdus kozodoii
serralysin-like metalloprotease
-
 Xenorhabdus kozodoii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Xenorhabdus kozodoii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5 8
-
 Xenorhabdus kozodoii