Detail Information of Xenobiotics

General Information of Xenobiotics (ID: XEO04051)
Xenobiotics Name
M-ctenitoxin-Cs1a
Xenobiotics Type
Amino Acid(s), Peptide(s) or Protein(s)
Classification
Peptide
DME(s) Modulated by This Xenobiotics
DME(s) Inhibited by This Xenobiotics
Azoreductase (azoR) DME Info Escherichia coli [1], [2]
Azoreductase (azoR) DME Info Enterococcus faecalis [1], [2]
L,D-carboxypeptidase A (ldcA) DME Info Escherichia coli [1], [2]
Beta-lactamase (blaB) DME Info Escherichia coli [1], [2]
Chloramphenicolase (chlR) DME Info Escherichia coli [1], [2]
Glycoside hydrolase (cscA) DME Info Escherichia coli [1], [2]
NADPH-dependent curcumin reductase (curA) DME Info Escherichia coli [1], [2]
Unclear metabolic mechanism (DME-unclear) DME Info Escherichia coli [1], [2]
Unclear metabolic mechanism (DME-unclear) DME Info Enterococcus faecalis [1], [2]
Glutamate decarboxylase (gadB) DME Info Escherichia coli [1], [2]
D-Lactate dehydrogenase (ldhA) DME Info Escherichia coli [1], [2]
D-Lactate dehydrogenase (ldhA) DME Info Pseudomonas aeruginosa [1], [2]
Molybdopterin-dependent enzyme (molD) DME Info Escherichia coli [1], [2]
Glutamate racemase (MurI) DME Info Escherichia coli [1], [2]
Arylamine N-acetyltransferase (NAT) DME Info Pseudomonas aeruginosa [1], [2]
N-ethylmaleimide reductase (nemA) DME Info Escherichia coli [1], [2]
NADPH-dependent oxidoreductase (nfrA) DME Info Staphylococcus aureus [1], [2]
Oxygen-insensitive NADPH nitroreductase A (nfsA) DME Info Escherichia coli [1], [2]
Oxygen-insensitive NADPH nitroreductase B (nfsB) DME Info Escherichia coli [1], [2]
NADH dehydrogenase (nuoE) DME Info Streptomyces griseus [1], [2]
Hydroxybenzoate 3-monooxygenase (pobA) DME Info Pseudomonas aeruginosa [1], [2]
Tyrosine decarboxylase (tdc) DME Info Enterococcus faecalis [1], [2]
Tyramine oxidase (tynA) DME Info Escherichia coli [1], [2]
Beta-glucuronidase (uidA) DME Info Escherichia coli [1], [2]
VanA ligase (vanA) DME Info Enterococcus faecalis [1], [2]
VanB ligase (vanB) DME Info Enterococcus faecalis [1], [2]
Xenobiotics-DME Activity Data
Xenobiotics-DME Activity Data Azoreductase (azoR) DME Info MIC = 0.31-0.63 microM [1], [2]
Azoreductase (azoR) DME Info MIC = 2.50-5.00 microM [1], [2]
L,D-carboxypeptidase A (ldcA) DME Info MIC = 0.31-0.63 microM [1], [2]
Beta-lactamase (blaB) DME Info MIC = 0.31-0.63 microM [1], [2]
Chloramphenicolase (chlR) DME Info MIC = 0.31-0.63 microM [1], [2]
Glycoside hydrolase (cscA) DME Info MIC = 0.31-0.63 microM [1], [2]
NADPH-dependent curcumin reductase (curA) DME Info MIC = 0.31-0.63 microM [1], [2]
Unclear metabolic mechanism (DME-unclear) DME Info MIC = 0.31-0.63 microM [1], [2]
Unclear metabolic mechanism (DME-unclear) DME Info MIC = 2.50-5.00 microM [1], [2]
Glutamate decarboxylase (gadB) DME Info MIC = 0.31-0.63 microM [1], [2]
D-Lactate dehydrogenase (ldhA) DME Info MIC = 0.31-0.63 microM [1], [2]
D-Lactate dehydrogenase (ldhA) DME Info MIC = 0.31-0.63 microM [1], [2]
Molybdopterin-dependent enzyme (molD) DME Info MIC = 0.31-0.63 microM [1], [2]
Glutamate racemase (MurI) DME Info MIC = 0.31-0.63 microM [1], [2]
Arylamine N-acetyltransferase (NAT) DME Info MIC = 0.31-0.63 microM [1], [2]
N-ethylmaleimide reductase (nemA) DME Info MIC = 0.31-0.63 microM [1], [2]
NADPH-dependent oxidoreductase (nfrA) DME Info MIC = 0.31-0.63 microM [1], [2]
Oxygen-insensitive NADPH nitroreductase A (nfsA) DME Info MIC = 0.31-0.63 microM [1], [2]
Oxygen-insensitive NADPH nitroreductase B (nfsB) DME Info MIC = 0.31-0.63 microM [1], [2]
NADH dehydrogenase (nuoE) DME Info MIC = 0.31-0.63 microM [1], [2]
Hydroxybenzoate 3-monooxygenase (pobA) DME Info MIC = 0.31-0.63 microM [1], [2]
Tyrosine decarboxylase (tdc) DME Info MIC = 2.50-5.00 microM [1], [2]
Tyramine oxidase (tynA) DME Info MIC = 0.31-0.63 microM [1], [2]
Beta-glucuronidase (uidA) DME Info MIC = 0.31-0.63 microM [1], [2]
VanA ligase (vanA) DME Info MIC = 2.50-5.00 microM [1], [2]
VanB ligase (vanB) DME Info MIC = 2.50-5.00 microM [1], [2]
References
1 Cupiennin 1, a new family of highly basic antimicrobial peptides in the venom of the spider Cupiennius salei (Ctenidae). J Biol Chem. 2002 Mar 29;277(13):11208-16.
2 Solution structure and interaction of cupiennin 1a, a spider venom peptide, with phospholipid bilayers. Biochemistry. 2007 Mar 20;46(11):3576-85.

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