EC                Enzyme                                 

gelatinase A;
72-kDa gelatinase;
matrix metalloproteinase 2;
type IV collagenase (ambiguous);
3/4 collagenase (obsolete);
matrix metalloproteinase 5 (obsolete);
72 kDa gelatinase type A;
collagenase IV (ambiguous);
collagenase type IV (ambiguous);
MMP 2;
type IV collagen metalloproteinase (ambiguous);
type IV collagenase/gelatinase (ambiguous)
Acting on peptide bonds (peptidases);
BRITE hierarchy
Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly!Ile-Ala-Gly-Gln
A secreted endopeptidase in peptidase family M10 (interstitial collagenase family), but possessing an additional fibronectin-like domain
EC created 1992
K01398  matrix metalloproteinase-2 (gelatinase A)
HSA: 4313(MMP2)
PTR: 454094(MMP2)
PPS: 100970966(MMP2)
GGO: 101147102(MMP2)
PON: 100451667(MMP2)
NLE: 100597186(MMP2)
MCC: 698478(MMP2)
MCF: 101865544(MMP2)
CSAB: 103233007(MMP2)
RRO: 104671481(MMP2)
RBB: 108531264(MMP2)
CJC: 100387448(MMP2)
SBQ: 101042210(MMP2)
MMU: 17390(Mmp2)
MCAL: 110299708(Mmp2)
MPAH: 110337240(Mmp2)
RNO: 81686(Mmp2)
MUN: 110545189(Mmp2)
CGE: 100774744(Mmp2)
NGI: 103731682(Mmp2)
HGL: 101696977(Mmp2)
CCAN: 109690723(Mmp2)
OCU: 100009000(MMP2)
TUP: 102483061(MMP2)
CFA: 403733(MMP2)
VVP: 112929621(MMP2)
AML: 100476183(MMP2)
UMR: 103673901(MMP2)
UAH: 113252249(MMP2)
ORO: 101378425(MMP2)
ELK: 111157340
FCA: 101098838(MMP2)
PTG: 102956398(MMP2)
PPAD: 109270907(MMP2)
AJU: 106973291(MMP2)
BTA: 282872(MMP2)
BOM: 102269336(MMP2)
BIU: 109572595(MMP2)
BBUB: 102401701(MMP2)
CHX: 102184364(MMP2)
OAS: 443115(MMP2)
SSC: 397391(MMP2)
CFR: 102511505 102521167(MMP2)
CDK: 105097506(MMP2)
BACU: 103016736(MMP2)
LVE: 103071760(MMP2)
OOR: 101275485(MMP2)
DLE: 111164984(MMP2)
PCAD: 102973920(MMP2)
ECB: 100033948(MMP2)
EPZ: 103553197(MMP2)
EAI: 106822484(MMP2)
MYB: 102260608(MMP2)
MYD: 102767174(MMP2)
MNA: 107543503(MMP2)
HAI: 109383663(MMP2)
DRO: 112296673(MMP2)
PALE: 102883808(MMP2)
RAY: 107499669(MMP2)
MJV: 108387896(MMP2)
LAV: 100659450(MMP2)
TMU: 101358817
MDO: 100020585(MMP2)
SHR: 100935012(MMP2)
PCW: 110207503(MMP2)
OAA: 100077120(MMP2)
GGA: 386583(MMP2)
MGP: 100125331(MMP2)
CJO: 107319190(MMP2)
NMEL: 110404299(MMP2)
APLA: 101802059(MMP2)
ACYG: 106043076(MMP2)
TGU: 100228546(MMP2)
LSR: 110484414(MMP2)
SCAN: 103816631(MMP2)
GFR: 102040497(MMP2)
FAB: 101815345(MMP2)
PHI: 102107059(MMP2)
PMAJ: 107209744(MMP2)
CCAE: 111934584(MMP2)
CCW: 104687474(MMP2)
ETL: 114060386(MMP2)
FPG: 101924896(MMP2)
FCH: 102056005(MMP2)
CLV: 102092170(MMP2)
EGZ: 104125198(MMP2)
NNI: 104016354(MMP2)
ACUN: 113484433(MMP2)
PADL: 103914183(MMP2)
AAM: 106483196(MMP2)
ASN: 102372370(MMP2)
AMJ: 102562302(MMP2)
PSS: 102463152(MMP2)
CMY: 102946066(MMP2)
CPIC: 101941088(MMP2)
ACS: 100557569(mmp2)
PVT: 110071465 110082478(MMP2)
PBI: 103055844(MMP2)
PMUR: 107295718(MMP2)
TSR: 106542288
PMUA: 114602200(MMP2)
GJA: 107108344(MMP2)
XLA: 380389(mmp2.S)
XTR: 548506(mmp2)
NPR: 108797889(MMP2)
DRE: 337179(mmp2)
SANH: 107657110(mmp2) 107696695
CCAR: 109092592
IPU: 108259638(mmp2)
PHYP: 113540866(mmp2)
EEE: 113590945(mmp2)
TRU: 653022(mmp2)
LCO: 104926945(mmp2)
NCC: 104964801(mmp2)
MZE: 101472680(mmp2)
ONL: 100700606(mmp2)
OLA: 100125419(mmp2)
XMA: 102226344(mmp2)
XCO: 114142975(mmp2)
PRET: 103462668(mmp2)
CVG: 107095465(mmp2)
NFU: 107381256(mmp2)
KMR: 108240277(mmp2)
ALIM: 106517245(mmp2)
AOCE: 111577723(mmp2)
CSEM: 103378988(mmp2)
POV: 109625153(mmp2)
LCF: 108876984(mmp2)
SDU: 111218486(mmp2)
SLAL: 111649502(mmp2)
HCQ: 109513920(mmp2)
BPEC: 110175240(mmp2)
MALB: 109955873(mmp2)
SASA: 100194903(mmp2) 106562416(MMP2)
ELS: 105023458(mmp2)
PKI: 111832721(mmp2) 111858175
LCM: 102350008(MMP2)
CMK: 103176101(mmp2)
RTP: 109921647(mmp2)
CIN: 100181993
 » show all
1  [PMID:2994741]
Murphy G, McAlpine CG, Poll CT, Reynolds JJ.
Purification and characterization of a bone metalloproteinase that degrades gelatin and types IV and V collagen.
Biochim Biophys Acta 831:49-58 (1985)
2  [PMID:2834383]
Collier IE, Wilhelm SM, Eisen AZ, Marmer BL, Grant GA, Seltzer JL, Kronberger A, He CS, Bauer EA, Goldberg GI.
H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen.
J Biol Chem 263:6579-87 (1988)
3  [PMID:2269296]
Okada Y, Morodomi T, Enghild JJ, Suzuki K, Yasui A, Nakanishi I, Salvesen G, Nagase H.
Matrix metalloproteinase 2 from human rheumatoid synovial fibroblasts. Purification and activation of the precursor and enzymic properties.
Eur J Biochem 194:721-30 (1990)
Other DBs
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IUBMB Enzyme Nomenclature:
ExPASy - ENZYME nomenclature database:
BRENDA, the Enzyme Database:
CAS: 146480-35-5

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