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EC Tree
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Cleavage of N-acetylmuramoyl-/-Ala, and of the insulin B chain at Gly23-/-Phe > Val18-/-Cya
Synonyms
Achromopeptidase component, beta-lytic metalloproteinase, beta-Lytic protease, blp, EC 3.4.99.13, EC3.4.24.4, Myxobacter AL-1 proteinase I, Myxobacter beta-lytic proteinase, Myxobacter495 beta-lytic proteinase, Myxobacterium sorangium beta-lytic proteinase,
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Achromopeptidase component
beta-lytic metalloproteinase
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EC3.4.24.4
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formerly included in
Myxobacter AL-1 proteinase I
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formerly EC 3.4.99.29
Myxobacter beta-lytic proteinase
Myxobacter495 beta-lytic proteinase
Myxobacterium sorangium beta-lytic proteinase
Proteinase, beta lytic metallo-
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Proteinase, Myxobacterium sorangium beta-lytic
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Achromopeptidase component
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Achromopeptidase component
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beta-Lytic protease
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Myxobacter beta-lytic proteinase
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Myxobacter beta-lytic proteinase
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Myxobacter495 beta-lytic proteinase
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Myxobacter495 beta-lytic proteinase
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Myxobacterium sorangium beta-lytic proteinase
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Myxobacterium sorangium beta-lytic proteinase
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Cleavage of N-acetylmuramoyl-/-Ala, and of the insulin B chain at Gly23-/-Phe > Val18-/-Cya
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hydrolysis of peptide bond
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3-(2-Furylacryloyl)-Gly-Leu amide + H2O
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Azocoll + H2O
Hydrolyzed azocoll
Bacterial cell walls + H2O
Hydrolyzed bacterial cell walls
Benzyloxycarbonyl-Gly-Phe amide + H2O
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casein + H2O
hydrolyzed casein
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limited activity
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DYMGWMDF-NH2 + H2O
DYMG + WMDF-NH2
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elastin-orcein + H2O
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Elastin-orcein + H2O
Hydrolyzed elastin-orcein
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furylacryloyl-Gly-Leu-NH2 + H2O
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GNLWATGHFM-NH2 + H2O
GNLWATG + HFM-NH2
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Insulin B-chain + H2O
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Insulin B-chain + H2O
Hydrolyzed insulin B-chain
KFIGLM-NH2 + H2O
KFIG + Leu-Met-NH2
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?
L-pyroglutamyl-HWSYGLRPG-NH2 + H2O
L-pyroglutamyl-HWSYG + LRPG-NH2
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L-pyroglutamyl-LM-NH2 + H2O
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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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RPPGFSPFR + H2O
RPPG + FSPFR
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WAGGDASGE + H2O
WAGG + DASGE
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WAGGNASGE + H2O
WAGG + NASGE
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Z-Gly-Phe-NH2 + H2O
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additional information
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Azocoll + H2O
Hydrolyzed azocoll
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Azocoll + H2O
Hydrolyzed azocoll
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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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pentaglycine + H2O
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pentaglycine + H2O
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peptidoglycan + H2O
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peptidoglycan + H2O
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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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no cleavage of Z-Gly-Phe
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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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additional information
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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 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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Zinc
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Lysobacter enzymogenes enzyme contains a zinc atom
Zn2+
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required for activity
Zn2+
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one zinc atom detected in the molecule by ion-spray mass spectrometry
Zn2+
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required for activity
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2-mercaptoethanol
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66% inhibition
1,10-phenanthroline
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90% inhibition
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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diisopropylfluorophosphate
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additional information
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insensitive to DFP
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additional information
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citrate; dinitrofluorobenzene; EDTA; iodoacetic acid; not: PCMB
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Encephalomyelitis, Autoimmune, Experimental
Treatment of an encephalitogenic peptide from guinea pig myelin basic protein with alpha-protease and thermolysin. Isolation of fragments and determination of cleavage sites.
Neoplasms
Synthesis and HPLC analysis of enzymatically cleavable linker consisting of poly(ethylene glycol) and dipeptide for the development of immunoconjugate.
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additional information
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10
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bacterial substrates
8.5 - 9
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bacteriolysis, Lysobacter enzymogenes
6.5
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3-(2-furylacryloyl)-Gly-Leu-amide, Lysobacter enzymogenes
6.5
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for FA-Gly-Leu-NH2 hydrolysis
9
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peptide substrates
9
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cell wall lysis, azocoll
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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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M497-1
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brenda
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brenda
three isozymes
UniProt
brenda
three isozymes
UniProt
brenda
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brenda
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brenda
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brenda
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brenda
M497-1
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brenda
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brenda
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brenda
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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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PRLB_ACHLY
374
1
40085
Swiss-Prot
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PRLB_LYSEN
178
0
19100
Swiss-Prot
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A0A1Z1NKI1_AERSA
387
0
42427
TrEMBL
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A0A0S2FCI9_9GAMM
387
1
41083
TrEMBL
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C7RB93_KANKD
Kangiella koreensis (strain DSM 16069 / KCTC 12182 / SW-125)
506
0
56361
TrEMBL
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D0IHD0_9VIBR
361
0
41120
TrEMBL
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A0A0S2G1X9_9GAMM
409
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43423
TrEMBL
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A0A650AXL2_9GAMM
378
1
40534
TrEMBL
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Q8RQS6_9GAMM
377
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40511
TrEMBL
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A0A653IU54_9MICC
86
0
9166
TrEMBL
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A0A0S2FLF7_9GAMM
378
1
40520
TrEMBL
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A0A0S2DCH3_LYSEN
377
0
40334
TrEMBL
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A0A6N9QLA8_9LEPT
336
1
37141
TrEMBL
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W0C1H2_9GAMM
374
0
39799
TrEMBL
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19350
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active enzyme, ion spray mass spectrometry
22000
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x * 22000 Achromobacter lyticus, SDS-PAGE
19100
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19100
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Lysobacter enzymogenes, calculated from amino acid sequence
19100
x * 19100, about, sequence calculation
19280
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acetonitrile-inactivated enzyme, ion spray mass spectrometry
19280
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calculated from the amino acid sequence deduced from the nucleotide sequence of the cloned blp gene
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?
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x * 22000 Achromobacter lyticus, SDS-PAGE
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x * 19100, about, sequence calculation
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x * 19100, about, sequence calculation
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3
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1 h, 95% loss of activity
31199
6.5 - 9.5
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45°C, 1 h, maximal stability
31199
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35
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0.02 M Tris-HCl, pH 9.0, 13% loss of activity after 8 h
40 - 50
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0.02 M Tris-HCl, pH 9.0, 70% loss of activity after 8 h
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4°C, 0.02 M Tris-HCl, pH 9.0, stable for at least 8 h
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partial purification from an extracellular sample by anion exchange chromatography
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DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree
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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 Arthrobacter globiformis, Micrococcus luteus and Staphylococcus aureus cells, inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent
additional information
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ability to lyse Micrococcus luteus and Staphylococcus aureus cells
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Jackson, R.L.; Matsueda, G.R.
Myxobacter AL-1 protease
Methods Enzymol.
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591-599
1970
unidentified myxobacterium, unidentified myxobacterium AL-1
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brenda
Li, S.L.; Norioka, S.; Sakiyama, F.
Molecular cloning and nucleotide sequence of the beta-lytic protease gene from Achromobacter lyticus
J. Bacteriol.
172
6506-6511
1990
Achromobacter lyticus, Lysobacter enzymogenes, Achromobacter lyticus M497-1
brenda
Kessler, E.
beta-Lytic endopeptidases
Methods Enzymol.
248
740-756
1995
Achromobacter lyticus, Lysobacter enzymogenes
brenda
Cruse, W.B.T.; Whitaker, D.R.
Preliminary crystallographic data for beta-lytic protease
J. Mol. Biol.
102
173-175
1976
unidentified myxobacterium, unidentified myxobacterium 495
brenda
Li, S.; Norioka, S.; Sakiyama, F.
Bacteriolytic activity and specificity of Achromobacter beta-lytic protease
J. Biochem.
124
332-339
1998
Achromobacter lyticus
brenda
Kessler, E.
Beta-lytic metalloendopeptidase
Handbook of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press
1
998-1000
2004
Achromobacter lyticus, Lysobacter enzymogenes
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brenda
Goekcen, A.; Vilcinskas, A.; Wiesner, J.
Biofilm-degrading enzymes from lysobacter gummosus
Virulence
5
378-387
2014
Lysobacter gummosus (W0C1H2), Lysobacter gummosus DSM Z 6980 (W0C1H2)
brenda
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