macrophage elastase | |||||||||
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Identifiers | |||||||||
EC no. | 3.4.24.65 | ||||||||
CAS no. | 146888-86-0 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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Matrix metalloproteinase-12 (MMP-12) also known as macrophage metalloelastase (MME) or macrophage elastase (ME) is an enzyme that in humans is encoded by the MMP12 gene.[5][6][7]
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins. The prodomain is cleaved by extracellular proteinases when the enzyme is activated. The active enzyme is constituted by two domains, the catalytic domain responsible for its enzymatic activity and the hemopexin-like domain that in some MMPs plays a role in substrate recognition and can contribute to increasing catalytic efficiency. It is thought that the protein encoded by this gene is cleaved at both ends to yield the active enzyme, but this processing has not been fully described. The enzyme degrades soluble and insoluble elastin. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.[5]
MMP12 may play a role in aneurysm formation[8] and studies in mice and humans suggest a role in the development of emphysema.[9]
PDB gallery
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1jiz: Crystal Structure Analysis of human Macrophage Elastase MMP-12
1jk3: Crystal structure of human MMP-12 (Macrophage Elastase) at true atomic resolution
1os2: Ternary enzyme-product-inhibitor complexes of human MMP12
1os9: Binary enzyme-product complexes of human MMP12
1rmz: Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor NNGH at 1.3 A resolution
1ros: Crystal structure of MMP-12 complexed to 2-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)ethyl-4-(4-ethoxy[1,1-biphenyl]-4-yl)-4-oxobutanoic acid
1utt: CRYSTAL STRUCTURE OF MMP-12 COMPLEXED TO 2-(1,3-DIOXO-1,3-DIHYDRO-2H-ISOINDOL-2-YL)ETHYL-4-(4-ETHOXY[1,1-BIPHENYL]-4-YL)-4-OXOBUTANOIC ACID
1utz: CRYSTAL STRUCTURE OF MMP-12 COMPLEXED TO (2R)-3-({[4-[(PYRI DIN-4-YL)PHENYL]-THIEN-2-YL}CARBOXAMIDO)(PHENYL)PROPANOIC ACID
1y93: Crystal structure of the catalytic domain of human MMP12 complexed with acetohydroxamic acid at atomic resolution
1ycm: Solution Structure of matrix metalloproteinase 12 (MMP12) in the presence of N-Isobutyl-N-[4-methoxyphenylsulfonyl]glycyl hydroxamic acid (NNGH)
1z3j: Solution Structure of MMP12 in the presence of N-isobutyl-N-4-methoxyphenylsulfonyl]glycyl hydroxamic acid (NNGH)
2hu6: Crystal structure of human MMP-12 in complex with acetohydroxamic acid and a bicyclic inhibitor
2oxu: Uninhibited form of human MMP-12
2oxw: Human MMP-12 complexed with the peptide IAG
2oxz: Human MMP-12 in complex with two peptides PQG and IAG
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