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Information on EC 3.4.24.76 - flavastacin
for references in articles please use BRENDA:EC3.4.24.76
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EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.24 Metalloendopeptidases
3.4.24.76 flavastacin
IUBMB Comments
A zinc metalloendopeptidase in peptidase family M12 (astacin family), secreted by the bacterium Flavobacterium meningosepticum . The specificity is similar to that of EC 3.4.24.33, peptidyl-Asp metalloendopeptidase from Pseudomonas fragi but the two are reported to be structurally dissimilar
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showHydrolyses polypeptides on the amino-side of Asp in -Xaa-/-Asp-. Acts very slowly on -Xaa-/-Glu
Synonyms
flavastacin, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
P40
additional information
-
peptidase family M12, member of the superfamily of the metzincins
P40
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolyses polypeptides on the amino-side of Asp in -Xaa-/-Asp-. Acts very slowly on -Xaa-/-Glu
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
167973-66-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Bovine serum albumin + H2O
?
Substrates: -
Products: -
Products: -
?
dansyl-Leu-(biantennary oligosaccharide)Asn-Asp-Ser-Arg-Val + H2O
dansyl-Leu-(biantennary oligosaccharide)Asn + Asp-Ser-Arg-Val
-
Substrates: -
Products: -
Products: -
?
furylacryloyl-Leu-Ala-Asp-Ala-Ala-NH2 + H2O
furylacryloyl-Leu-Ala + Asp-Ala-Ala-NH2
-
Substrates: -
Products: -
Products: -
?
N-glycosylated asparagine in glycoproteine + H2O
?
Substrates: tryptic fragments. The enzyme shows unique cleavage specificity towards the C-terminus of N-glycosylated asparagine residues (N156)
Products: -
Products: -
?
NGSDCPDK + H2O
L-Asn + GSDCPDK
Substrates: -
Products: -
Products: -
?
PFLNWTGPPEPIEAAVAR + H2O
PFLN + WTGPPEPIEAAVAR
Substrates: -
Products: -
Products: -
?
TAGWNIPMGLLFNQTGSCK + H2O
TAGWNIPMGLLFN + QTGSCK
Substrates: -
Products: -
Products: -
?
TAGWNVPIGTLRPFLNWTGPPEPIEAAVAR + H2O
TAGWNVPIGTLRPFLN + WTGPPEPIEAAVAR
Substrates: -
Products: -
Products: -
?
furylacryloyl-Leu-Ala-Asp-Ala-Ser-NH2 + H2O
furylacryloyl-Leu-Ala + Asp-Ser-Ala-NH2
-
Substrates: -
Products: -
Products: -
?
furylacryloyl-Leu-Ala-Asp-Ala-Ser-NH2 + H2O
furylacryloyl-Leu-Ala + Asp-Ser-Ala-NH2
-
Substrates: hydrolyzes peptides on the N-terminal side of aspartic acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: aspargine and glutamine analogs not hydrolyzed, at high enzyme concentrations slow cleavage of the glutamic acid analog
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme works only on peptides smaller than 50 amino acids and has no specificity for the N-terminus of aspartic acid
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
-
activation accomplished by dialysis against 1 mM zinc acetate
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SPECIFIC ACTIVITY [µmol/min/mg]
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
Highest Expressing Human Cell Lines
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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). A0A2Z2NS79_9GAMM
446
0
47809
TrEMBL
-
A0A376DMG9_9FLAO
443
0
48935
TrEMBL
-
A0A1V5S870_9BACT
395
0
45321
TrEMBL
-
C2G5R1_SPHSI
220
0
24524
TrEMBL
-
A0A2Z2P5Q2_9GAMM
496
0
53672
TrEMBL
-
A0A1Q2HMD1_9BACT
460
0
50729
TrEMBL
-
A0A1V6CUD2_9BACT
934
0
103281
TrEMBL
-
G0L9S4_ZOBGA
Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij)
358
0
39797
TrEMBL
-
A0A1V5RZQ8_9BACT
384
0
44346
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38840
40090
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
-
O-linked heptasaccharide attached to Ser264 containing uronic acids and methylated sugars
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to homogeneity by hydrophobic interaction chromatography in the presence of 10 mM EDTA to avoid autoproteolysis
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tarentino, A.L.; Quinones, G.; Grimwood, B.G.; Hauer, C.R.; Plummer, T.H.
Molecular cloning and sequence analysis of flavastacin: an O-glycosylated prokaryotic zinc metalloendopeptidase
Arch. Biochem. Biophys.
319
281-285
1995
Elizabethkingia meningoseptica
brenda
Tarentino, A.L.
Flavastacin
Handbook Of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press
1
631-632
2004
Elizabethkingia meningoseptica
-
brenda
Pralow, A.; Hoffmann, M.; Nguyen-Khuong, T.; Rapp, E.; Reichl, U.
Improvement of the glycoproteomic toolbox with the discovery of a unique C-terminal cleavage specificity of flavastacin for N-glycosylated asparagine
Sci. Rep.
7
11419
2017
Elizabethkingia meningoseptica (Q47899)
brenda
EXTERNAL LINKS (specific for EC-Number 3.4.24.76)
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Release 2023.1 (January 2023)
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