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Information on EC 3.4.24.35 - gelatinase B and Organism(s) Gallus gallus
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3.4.24.35 gelatinase BSpecify your search results
Word Map
- 3.4.24.35
- mmp-2
- metalloproteinases
-
zymography
- metastasis
- timp-1
- endothelial
- necrosis
- angiogenesis
- tnf
- artery
- fibrosis
- neutrophil
- chemokine
- infarct
- plaque
- monocyte
- vessel
- pulmonary
- myocardial
- cerebral
- mapks
- stroke
- erk
-
transwell
-
basement
- aortic
-
invasiveness
- plasminogen
-
blood-brain
- matrigel
- bcl-2
- nf-kappab
- airway
- upa
- osteoclast
- cox-2
- fibronectin
- aneurysm
-
c-reactive
- mt1-mmp
- e-cadherin
- coronary
- tnf-alpha
-
angiogenic
- atherosclerotic
-
anti-metastatic
-
tartrate-resistant
-
urokinase-type
- drug development
- diagnostics
- elastin
- rankl
- medicine
The taxonomic range for the selected organisms is: Gallus gallus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
mmp-9, matrix metalloproteinase-9, matrix metalloproteinase 9, gelatinase b, matrix metallopeptidase 9, matrix metalloprotease-9, mmp 9, 92-kda gelatinase, 92 kda gelatinase, 92-kda type iv collagenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
92 kDa gelatinase
-
-
-
-
92-kDa Gelatinase
-
-
-
-
92-kDa Type IV collagenase
-
-
-
-
95 kDa type IV collagenase/gelatinase
-
-
-
-
Collagenase IV
-
-
-
-
Collagenase type IV
-
-
-
-
gelatinase
Gelatinase MMP 9
-
-
-
-
GELB
-
-
-
-
Macrophage gelatinase
-
-
-
-
Matrix metalloproteinase 9
MMP 9
-
-
-
-
MMP-9
MMP9
Type IV collagen metalloproteinase
-
-
-
-
Type IV collagenase
-
-
-
-
Type IV collagenase/gelatinase
-
-
-
-
Type V collagenase
-
-
-
-
Matrix metalloproteinase 9
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
146480-36-6
-
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
(7-methoxy-coumarin-4-yl)acetyl-PLGL-beta-(2,4-dinitrophenylamino)-AAR-NH2 + H2O
(7-methoxy-coumarin-4-yl)acetyl-PL + GL-beta-(2,4-dinitrophenylamino)-AAR-NH2
-
-
-
-
?
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
tissue inhibitor of metalloproteinases 1
-
TIMP-1, complete inhibition at 0.5 mg
-
tissue inhibitor of metalloproteinases 2
-
TIMP-2, complete inhibition at 0.5 mg
-
additional information
-
the 230 kDa enzyme does not remain intact in 4 M urea, 0.5 M NaCl, 4 M CsCl or 4 M GdHCl. Glycosaminoglycan chains may interfere with inhibitors
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
distribution of MMP9 in both emigrating and migrating neural crest cells, overview
gene MMP9 is significantly upregulated in 23-wk-old (laying phase) chicken ovaries compared with 6-wk-old ovaries (prepubertal phase). In reproductively active chicken ovary, the enzyme expression level increases during follicular maturation. Enzyme MMP9 mRNA expression continues to rise in postovulatory follicle 1 and postovulatory follicle 2 after ovulation
infundibulum, magnum, isthmus, and shell gland. Developmental changes, overview
additional information
additional information
immunohistochemic localization analysis, overview
additional information
quantitative enzyme tissue expression analysis in the chicken oviduct during maturation
additional information
-
quantitative enzyme tissue expression analysis in the chicken oviduct during maturation
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
enzyme localization and comparison to other MMPs, immunohistochemic analysis
-
additional information
-
enzyme localization and comparison to other MMPs, immunohistochemic analysis
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
enzyme inhibition prevents neural crest cells delamination and migration
physiological function
additional information
physiological function
-
enzyme matrix metalloproteinase 9/gelatinase B is required for neural crest cell migration, which are neuroepithelial progenitors that convert into mesenchyme and migrate along defined paths throughout the embryo. The enzyme plays a role during neural crest cell detachment from the neural tube, overview
physiological function
potential role of the MMP system in avian oviduct development, avian reproductive system differs from that of mammals. The gelatinases, stromelysins and matrilysins, all belonging to the MMP family, are capable of degrading major constituents of basement membranes, including type IV collagen, laminin and fibronectin. Gelatinolytic activity of MMPs in the chicken oviduct during maturation, overview
additional information
-
digestion of the intact enzyme with chondroitinase decreases the size of the molecule to 80 kDa
additional information
-
enzyme MMP9 promotes neural crest cell emigration from the neural tube by enhancing breakage of laminin at the basement-membrane, mechanism of activity, overview
additional information
enzymes MMP1, MMP3, and MMP9 are synthesized and secreted by granulosa cells of different follicles in the chicken ovary, overview. The three MMP genes (MMP1, MMP3, and MMP9) are significantly upregulated in 23-wk-old (laying phase) chicken ovaries compared with 6-wk-old ovaries (prepubertal phase). In reproductively active chicken ovary, MMP1 expression (both mRNA and protein) remains low in prehierarchical and preovulatory follicles but increases in postovulatory follicles (POFs). Both MMP3 and MMP9 expression levels increase during follicular maturation. MMP3 reaches maximal expression in the first largest follicle (F1), while MMP9 levels continue to rise in POF1 and POF2 after ovulation
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). A0A3Q2U2B5_CHICK
713
0
78338
TrEMBL
Secretory Pathway (Reliability: 1)
F1NGT3_CHICK
688
0
76857
TrEMBL
Secretory Pathway (Reliability: 1)
Q9DE15_CHICK
686
0
76680
TrEMBL
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
230000
-
x * 80000, deglycosylated enzyme, SDS-PAGE, x * 230000, glycosylated enzyme, SDS-PAGE
80000
-
x * 80000, deglycosylated enzyme, SDS-PAGE, x * 230000, glycosylated enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 80000, deglycosylated enzyme, SDS-PAGE, x * 230000, glycosylated enzyme, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
the enzyme contains covalently bound glycosaminoglycan i.e. chondroitin sulfate chains, deglycosylation by protease-free chondroitinase ABC
additional information
-
digestion of the intact enzyme with chondroitinase decreases the size of the molecule to 80 kDa
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the 230 kDa enzyme does not remain intact in 4 M urea, 0.5 M NaCl, 4 M CsCl or 4 M GdHCl
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from tibia by gelatin-agarose affinity chromatography, anion exchange chromatography, and dialysis
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene MMP9, cloning of an enzyme fragment, containing an ATG start codon, signal peptide, prodomain sequence, active site, fibronectin II repeat domain and zinc binding sequence,from chondrocyte cDNA, stable recombinant expression in a rat chondrosarcoma cell line
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme expression is induced in chick embryonic tibias cultured with lipopolysaccharide
-
the mRNA of MMP9 in the granulosa cells is induced by TGFB1 but not follicle-stimulating hormone, luteinizing hormone, progesterone, or estrogen. Luciferase reporter and mutagenesis analysis indicate the AP1 and NFkappaB elements located in the promoter region from -1700 to -2400 bp are critical for both basal and TGFB1-induced MMP9 transcription
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Patchigolla, R.; Knudson, W.; Schmid, T.
Matrix metalloproteinase-9 in a unique proteoglycan form in avian embryonic growth plate cartilage
Arch. Biochem. Biophys.
520
42-50
2012
Gallus gallus
Zhu, G.; Kang, L.; Wei, Q.; Cui, X.; Wang, S.; Chen, Y.; Jiang, Y.
Expression and regulation of MMP1, MMP3, and MMP9 in the chicken ovary in response to gonadotropins, sex hormones, and TGFB1
Biol. Reprod.
90
57
2014
Gallus gallus (F1NGT3), Gallus gallus White leghorn (F1NGT3)
Monsonego-Ornan, E.; Kosonovsky, J.; Bar, A.; Roth, L.; Fraggi-Rankis, V.; Simsa, S.; Kohl, A.; Sela-Donenfeld, D.
Matrix metalloproteinase 9/gelatinase B is required for neural crest cell migration
Dev. Biol.
364
162-177
2012
Gallus gallus, Gallus gallus Lohman
Lesniak-Walentyn, A.; Hrabia, A.
Expression and localization of matrix metalloproteinases (MMP-2, -7, -9) and their tissue inhibitors (TIMP-2, -3) in the chicken oviduct during maturation
Cell Tissue Res.
364
185-197
2016
Gallus gallus (Q9DE15), Gallus gallus, Gallus gallus Hy-Line Brown (Q9DE15)
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