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Information on EC 3.4.24.32 - beta-Lytic metalloendopeptidase
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3.4.24.32 beta-Lytic metalloendopeptidaseSpecify your search results
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- 3.4.24.32
-
3.4.24.4
- thermolysin
- achromobacter
- lyticus
-
bacteriolytic
-
thermoproteolyticus
- biotechnology
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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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Achromopeptidase component
beta-Lytic protease
Myxobacter beta-lytic proteinase
Myxobacter495 beta-lytic proteinase
Myxobacterium sorangium beta-lytic proteinase
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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
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CAS REGISTRY NUMBER
COMMENTARY
37288-92-9
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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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-
?
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NATURAL SUBSTRATE
NATURAL 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
additional information
?
-
-
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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-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
Zn2+
-
one zinc atom detected in the molecule by ion-spray mass spectrometry
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
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
-
citrate; dinitrofluorobenzene; EDTA; iodoacetic acid; not: PCMB
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
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
-
a biofilm-degrading enzyme, overview. Degradation of biofilms formed by e.g. Staphylococcus epidermidis strain RP62A
additional information
enzyme identification by peptide mass fingerprinting
additional information
-
enzyme identification by peptide mass fingerprinting
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A6N9QLA8_9LEPT
336
1
37141
TrEMBL
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C7RB93_KANKD
Kangiella koreensis (strain DSM 16069 / KCTC 12182 / SW-125)
506
0
56361
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
19100
19280
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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SUBUNIT
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
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
-
ability to lyse Micrococcus luteus and Staphylococcus aureus cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jackson, R.L.; Matsueda, G.R.
Myxobacter AL-1 protease
Methods Enzymol.
19
591-599
1970
unidentified myxobacterium, unidentified myxobacterium AL-1
-
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
-
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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