• DRAMP ID

    • DRAMP03666
    • Peptide Name

    • N-acetylmuramoyl-L-alanine amidase L2
    • Source

    • Lysobacter sp.
    • Family

    • Not found
    • Gene

    • Not found
    • Sequence

    • XNVVFLNXPXPQW
    • Sequence Length

    • 13
    • Protein Existence

    • Protein level
    • Biological Activity

    • Antimicrobial, Antibacterial
    • Target Organism

    • No MICs found in DRAMP database
    • Hemolytic Activity

      • No hemolysis information or data found in the reference(s) presented in this entry
    • Cytotoxicity

      • Not included yet
    • Binding Target

    • Not found
    • Linear/Cyclic

    • Not included yet
    • N-terminal Modification

    • Not included yet
    • C-terminal Modification

    • Not included yet
    • Nonterminal Modifications and Unusual Amino Acids

    • Not included yet
    • Stereochemistry

    • Not included yet
    • Structure

    • Not found
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP03666 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP03666.
    • Formula

    • C59H78N14O11
    • Absent Amino Acids

    • ACDEGHIKMRSTY
    • Common Amino Acids

    • X
    • Mass

    • 1547.39
    • PI

    • 5.52
    • Basic Residues

    • 0
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 5
    • Net Charge

    • 0
    • Boman Index

    • -0.51
    • Hydrophobicity

    • 0.031
    • Aliphatic Index

    • 74.62
    • Half Life

      • Mammalian:?
      • Yeast:?
      • E.coli:?
    • Extinction Coefficient Cystines

    • 5500
    • Absorbance 280nm

    • 458.33
    • Polar Residues

    • 2

DRAMP03666

    • Biophysicochemical properties

    • Optimum pH is 8.0; Optimum temperature is 65 degrees Celsius.
    • Also has Catalytic activity

    • Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
  • ·Literature 1
    • Title

    • Identification of extracellular bacteriolytic enzymes from Lysobacter sp. XL1.
    • Reference

    • Submitted (APR-2007) to UniProtKB.
    • Author

    • Muranova T.A, Stepnaya O.A, Tsfasman I.M, Kulaev I.S.