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Enzyme Nomenclature
Information on EC 3.4.24.32 - beta-Lytic metalloendopeptidase
for references in articles please use BRENDA:EC3.4.24.32
Word Map on EC 3.4.24.32
- 3.4.24.32
- achromobacter
- lyticus
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bacteriolytic
- lysozyme
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alpha-lytic
- lysobacter
- 1,10-phenanthroline
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lysed
- biotechnology
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
3.4.24.32
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RECOMMENDED NAME
GeneOntology No.
beta-Lytic metalloendopeptidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cleavage of N-acetylmuramoyl-/-Ala, and of the insulin B chain at Gly23-/-Phe > Val18-/-Cya
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY
37288-92-9
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
physiological function
a biofilm-degrading enzyme, overview. Degradation of biofilms formed by e.g. Staphylococcus epidermidis strain RP62A
physiological function
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a biofilm-degrading enzyme, overview. Degradation of biofilms formed by e.g. Staphylococcus epidermidis strain RP62A
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additional information
enzyme identification by peptide mass fingerprinting
additional information
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enzyme identification by peptide mass fingerprinting
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-pyroglutamyl-HWSYGLRPG-NH2 + H2O
L-pyroglutamyl-HWSYG + LRPG-NH2
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?
L-pyroglutamyl-QRLGNQWAVGHLM-NH2 + H2O
L-pyroglutamyl-QRLG + NQWAVGHLM-NH2
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?
L-pyroglutamyl-VPQWAVGHFM-NH2 + H2O
L-pyroglutamyl-VPQWAVG + HFM-NH2
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?
Bacterial cell walls + H2O
Hydrolyzed bacterial cell walls
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cleaves specific peptide bonds within the cell wall peptidoglycan network
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Bacterial cell walls + H2O
Hydrolyzed bacterial cell walls
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Lysobacter enzymogenes enzyme: Arthrobacter globiformis cells
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Bacterial cell walls + H2O
Hydrolyzed bacterial cell walls
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Micrococcus lysodeikticus cells
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Bacterial cell walls + H2O
Hydrolyzed bacterial cell walls
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Arthrobacter crystallopoietes cells walls
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Bacterial cell walls + H2O
Hydrolyzed bacterial cell walls
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Arthrobacter crystallopoietes cells walls
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Insulin B-chain + H2O
Hydrolyzed insulin B-chain
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does not act on A-chain of oxidized insulin, it cleaves the B-chain readily at Gly23-Phe24 and more slowly at Val18-Cys19-SO3H
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Insulin B-chain + H2O
Hydrolyzed insulin B-chain
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hydrolysis of Ala-Leu bond
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Insulin B-chain + H2O
Hydrolyzed insulin B-chain
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hydrolysis of Ala-Leu bond
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additional information
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the primary biological role is the defense against bacteria in the environment, in particular against species of Staphylococcus or closely related organisms
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additional information
?
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the enzyme only cleaves Gly-X bonds and favors hydrophobic or apolar residues to either side, it does not hydrolyze bonds with charged amino acids or proline adjacent, cleaves D-Ala-Gly and D-Ala-Ala bonds in the linkage between peptide subunit and the interpeptide bridge and also the Gly-Gly bond in the Staphylococcus aureus interpeptide bridge
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additional information
?
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the primary biological role is the defense against bacteria in the environment, in particular against species of Staphylococcus or closely related organisms
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additional information
?
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affinity towards peptide bonds formed by at least one hydrophobic amino acid in a structure at least as large as a tetrapeptide
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additional information
?
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affinity towards peptide bonds formed by at least one hydrophobic amino acid in a structure at least as large as a tetrapeptide
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
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the primary biological role is the defense against bacteria in the environment, in particular against species of Staphylococcus or closely related organisms
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additional information
?
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the primary biological role is the defense against bacteria in the environment, in particular against species of Staphylococcus or closely related organisms
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
Zn2+
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one zinc atom detected in the molecule by ion-spray mass spectrometry
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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only 2% inhibition with EDTA, no inhibition with diisopropyl fluorophosphate, phenylmethylsulfonyl fluoride, iodoacetate, phosphoramidon, N-chloroacetyl-N-hydroxy-leucyl-Ala-Gly-NH2, chymostatin, elastinal, leupeptin, and pepstatin
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additional information
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citrate; dinitrofluorobenzene; EDTA; iodoacetic acid; not: PCMB
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10.5
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exhibits higher bacteriolytic activity at pH 10.0 than at pH 7.0-9.0
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
19100
19280
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acetonitrile-inactivated enzyme, ion spray mass spectrometry; calculated from the amino acid sequence deduced from the nucleotide sequence of the cloned blp gene
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial purification from an extracellular sample by anion exchange chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
additional information
biotechnology
extracellular digestion of biofilms by Lysobacter gummosus depends on multiple bacteriolytic and proteolytic enzymes, which can be exploited for biofilm control, a following gel filtration step highly reduces enzyme activity
biotechnology
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extracellular digestion of biofilms by Lysobacter gummosus depends on multiple bacteriolytic and proteolytic enzymes, which can be exploited for biofilm control, a following gel filtration step highly reduces enzyme activity
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additional information
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ability to lyse Micrococcus luteus and Staphylococcus aureus cells
additional information
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ability to lyse Arthrobacter globiformis, Micrococcus luteus and Staphylococcus aureus cells, inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent
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LINKS TO OTHER DATABASES (specific for EC-Number 3.4.24.32)
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