General Information of Xenobiotics (ID: XEO02317)
Xenobiotics Name
Arenicin-1
Xenobiotics Type
Amino Acid(s), Peptide(s) or Protein(s)
Classification
Peptide
DME(s) Modulated by This Xenobiotics
DME(s) Inhibited by This Xenobiotics
Aminoglycoside adenylyltransferase (aadA1a) DME Info Salmonella enterica [1], [2]
Azoreductase (azoR) DME Info Escherichia coli [1], [2]
L,D-carboxypeptidase A (ldcA) DME Info Escherichia coli [1], [2]
Beta-lactamase (blaB) DME Info Escherichia coli [1], [2]
New delhi metallo-beta-lactamase NDM-1 (blaNDM) DME Info Salmonella enterica [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]
Glutamate decarboxylase (gadB) DME Info Listeria monocytogenes [1], [2]
Glutamate decarboxylase (gadB) DME Info Escherichia coli [1], [2]
D-Lactate dehydrogenase (ldhA) DME Info Escherichia coli [1], [2]
Homoserine-O-transsuccinylase (metAA) DME Info Salmonella enterica [1], [2]
Molybdopterin-dependent enzyme (molD) DME Info Escherichia coli [1], [2]
Glutamate racemase (MurI) DME Info Escherichia coli [1], [2]
N-ethylmaleimide reductase (nemA) DME Info Escherichia coli [1], [2]
Oxygen-insensitive NADPH nitroreductase A (nfsA) DME Info Escherichia coli [1], [2]
Oxygen-insensitive NADPH nitroreductase A (nfsA) DME Info Salmonella enterica [1], [2]
Oxygen-insensitive NADPH nitroreductase B (nfsB) DME Info Escherichia coli [1], [2]
Oxygen-insensitive NADPH nitroreductase B (nfsB) DME Info Salmonella enterica [1], [2]
Arylamine N-acetyltransferase (NAT) DME Info Salmonella enterica [1], [2]
NADH dehydrogenase (nuoE) DME Info Streptomyces griseus [1], [2]
Tyramine oxidase (tynA) DME Info Escherichia coli [1], [2]
Beta-glucuronidase (uidA) DME Info Escherichia coli [1], [2]
Nitroreductase (NTR) DME Info Salmonella enterica [1], [2]
Nitroreductase (NTR) DME Info Salmonella typhimurium [1], [2]
Xenobiotics-DME Activity Data
Xenobiotics-DME Activity Data Aminoglycoside adenylyltransferase (aadA1a) DME Info MIC = 300 microM [1], [2]
Azoreductase (azoR) DME Info MIC = 300 microM [1], [2]
L,D-carboxypeptidase A (ldcA) DME Info MIC = 300 microM [1], [2]
Beta-lactamase (blaB) DME Info MIC = 300 microM [1], [2]
New delhi metallo-beta-lactamase NDM-1 (blaNDM) DME Info MIC = 300 microM [1], [2]
Chloramphenicolase (chlR) DME Info MIC = 300 microM [1], [2]
Glycoside hydrolase (cscA) DME Info MIC = 300 microM [1], [2]
NADPH-dependent curcumin reductase (curA) DME Info MIC = 300 microM [1], [2]
Unclear metabolic mechanism (DME-unclear) DME Info MIC = 300 microM [1], [2]
Glutamate decarboxylase (gadB) DME Info MIC = 0.6 ug/ml [1], [2]
Glutamate decarboxylase (gadB) DME Info MIC = 300 microM [1], [2]
D-Lactate dehydrogenase (ldhA) DME Info MIC = 300 microM [1], [2]
Homoserine-O-transsuccinylase (metAA) DME Info MIC = 300 microM [1], [2]
Molybdopterin-dependent enzyme (molD) DME Info MIC = 300 microM [1], [2]
Glutamate racemase (MurI) DME Info MIC = 300 microM [1], [2]
N-ethylmaleimide reductase (nemA) DME Info MIC = 300 microM [1], [2]
Oxygen-insensitive NADPH nitroreductase A (nfsA) DME Info MIC = 300 microM [1], [2]
Oxygen-insensitive NADPH nitroreductase A (nfsA) DME Info MIC = 300 microM [1], [2]
Oxygen-insensitive NADPH nitroreductase B (nfsB) DME Info MIC = 300 microM [1], [2]
Oxygen-insensitive NADPH nitroreductase B (nfsB) DME Info MIC = 300 microM [1], [2]
Arylamine N-acetyltransferase (NAT) DME Info MIC = 300 microM [1], [2]
NADH dehydrogenase (nuoE) DME Info MIC = 300 microM [1], [2]
Tyramine oxidase (tynA) DME Info MIC = 300 microM [1], [2]
Beta-glucuronidase (uidA) DME Info MIC = 300 microM [1], [2]
Nitroreductase (NTR) DME Info MIC = 300 microM [1], [2]
Nitroreductase (NTR) DME Info MIC = 300 microM [1], [2]
References
1 Purification and primary structure of two isoforms of arenicin, a novel antimicrobial peptide from marine polychaeta Arenicola marina. FEBS Lett. 2004 Nov 5;577(1-2):209-14.
2 Structure and mode of action of the antimicrobial peptide arenicin. Biochem J. 2008 Feb 15;410(1):113-22.

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