Family M10


Summary Holotypes Alignment Tree Genomes Structure Literature H-seq M-seq Architecture


Summary Holotypes Alignment Tree Genomes Literature


Summary Holotypes Alignment Tree Genomes Literature


Summary Holotypes Alignment Tree Genomes Literature

Summary for family M10

Family type peptidaseM10.001 - matrix metallopeptidase-1 (Homo sapiens), MEROPS Accession MER0001063 (peptidase unit: 98-276)
Content of familyPeptidase family M10 contains metalloendopeptidases.
History Identifier created: Biochem.J. 290:205-218 (1993)
Catalytic typeMetallo
Active siteThe zinc ligands and catalytic glutamate of family M10 occur in the motif HEXXHXXGXXH, as in families M12, M43 and M57.
Activities and specificitiesLike other peptidases in subclan MA(M), the peptidases of family M10 are synthesized as inactive precursors. However, differences exist in the mechanisms of activation. The inactivity of the proenzymes of the matrixins in subfamily M10A is due to what is known as a "cysteine switch" (Van Wart & Birkedal-Hansen, 1990). In this, there is an interaction between a conserved cysteine in the propeptide and the catalytic zinc in the ion that prevents the binding of a crucial water molecule. Because of the importance of cysteine in the latency of the proenzymes, they can commonly be activated by thiol-blocking agents such as aminophenylmecuric acetate (APMA). Serralysin, and activation of the proenzyme is by removal of an N-terminal propeptide.
InhibitorsLike other metallopeptidases, the peptidases in family M10 are inhibited by chelating agents, and many potent inhibitors such as batimastat have been synthesized as possible drugs. The timp proteins in family I35 inhibit the peptidases of subfamily M10A, but not M10B. Serralysin is inhibited by a 10kDa inhibitor from Serratia (I38.003).
Molecular structureThe peptidases of family M10 belong to a group of peptidases known as the "metzincins", due to a conserved methionine C-terminal to the zinc ligands which forms what is known as a "Met-turn" (Bode et al., 1993). Both subfamilies of M10 contain mosaic proteins. Serralysin contains a glycine-rich C-terminal domain Gly-Gly-Xaa-Gly-Asn-Asp which has a role in binding calcium ions. The matrixins possess at least one C-terminal domain homologous to hemopexin and vitronectin, thought to help the enzyme bind to the extracellular matrix. The gelatinases have acquired three domains homologous to type II segments of fibronectin nested within the peptidases unit.
Basis of clan assignmentProtein fold of the peptidase unit for members of this family resembles that of thermolysin, the type example for clan MA.
Distribution of family Bacteria details  
Archaea details  
Protozoa details  
Fungi -  
Plants details  
Animals details  
Viruses details  
Biological functionsThe matrixins in family M10 are mostly secreted proteins that function extracellularly. The matrixins in subfamily M10A are synthesized with conventional signal peptides, but the bacterial serralysin in subfamily M10B is synthesized without a signal peptide, and is secreted by a different mechanism. The matrixins play important roles in the degradation of connective tissue matrix proteins and both in normal tissue turnover and in pathological tissue damage.
Pharmaceutical and biotech relevanceThe matrixins in family M10 are drug targets for prevention of pathological tissue damage an tumour invasion (Heath & Grochow, 2000).
Statistics for family M10Sequences:12952
Identifiers with PDB entries:21
Downloadable files Sequence library (FastA format)
Sequence alignment (FastA format)
Phylogenetic tree (Newick format)
Other databases INTERPRO IPR002510
PFAM PF01523
PFAM PF10263
PFAM PF12315
SCOP 111284
Subfamily M10A
Name Peptidase subfamily M10A
Subfamily type peptidase M10.001 - matrix metallopeptidase-1 (Homo sapiens), MEROPS Accession MER0001063 (peptidase unit: 98-276)
Active site residues H218 E219 H222 H228 
Statistics Sequences: 10551
Identifiers: 52
Identifiers with PDB entries: 15
Other databases CATH 3.40.390.10
PFAM PF00413
SCOP 55528
Downloadable files Sequence library [FastA format]
Sequence alignment [FastA format]
Phylogenetic tree [Newick format]
Peptidases and Homologues MEROPS ID Structure
matrix metallopeptidase-1M10.001Yes
matrix metallopeptidase-8M10.002Yes
matrix metallopeptidase-2M10.003Yes
matrix metallopeptidase-9M10.004Yes
matrix metallopeptidase-3M10.005Yes
matrix metallopeptidase-10 (Homo sapiens-type)M10.006Yes
matrix metallopeptidase-11M10.007Yes
matrix metallopeptidase-7M10.008Yes
matrix metallopeptidase-12M10.009Yes
matrix metallopeptidase-10 (rodent type)M10.011-
GM1-MMP (Glycine max)M10.012-
matrix metallopeptidase-13M10.013Yes
membrane-type matrix metallopeptidase-1M10.014Yes
membrane-type matrix metallopeptidase-2M10.015-
membrane-type matrix metallopeptidase-3M10.016Yes
membrane-type matrix metallopeptidase-4M10.017-
matrix metallopeptidase-18M10.018-
matrix metallopeptidase-20M10.019Yes
matrix metallopeptidase-19M10.021-
matrix metallopeptidase-23BM10.022Yes
membrane-type matrix metallopeptidase-5M10.023-
membrane-type matrix metallopeptidase-6M10.024-
HMMP (Hydra vulgaris)-like peptidaseM10.025-
matrix metallopeptidase-21M10.026-
matrix metallopeptidase-22M10.027-
matrix metallopeptidase-26M10.029-
matrix metallopeptidase-28M10.030-
Dm1 matrix metallopeptidaseM10.031-
matrixin VM10.032-
collagenase-like A peptidase (rodent)M10.033-
collagenase-like B peptidase (rodent)M10.034-
Dm2-matrix metallopeptidaseM10.036-
matrix metallopeptidase-23AM10.037-
At5-MMP (Arabidopsis thaliana)M10.038-
Cydia pomonella granulovirus metallopeptidaseM10.040-
Pta1 peptidaseM10.065-
Zmp-1 peptidase (Caenorhabditis-type)M10.067-
Zmp-2 peptidase (Caenorhabditis sp.)M10.068-
macrophage elastase homologue (chromosome 8, Homo sapiens)M10.950-
Mername-AA156 proteinM10.971-
matrix metallopeptidase-like 1M10.973-
similar to matrix metallopeptidase 25 (Rattus norvegicus)M10.974-
At2-MMP (Arabidopsis thaliana)M10.A01-
At4-MMP (Arabidopsis thaliana)M10.A02-
At1-MMP (Arabidopsis thaliana)M10.A04-
At3-MMP (Arabidopsis thaliana)M10.A05-
Mername-AA284 peptidaseM10.A06-
Zmp-3 (Caenorhabditis elegans)M10.A07-
Zmp-4 (Caenorhabditis elegans)M10.A08-
Zmp-5 (Caenorhabditis elegans)M10.A09-
Zmp-6 (Caenorhabditis elegans)M10.A10-
Subfamily M10A non-peptidase homologuesnon-peptidase homologue-
Subfamily M10A unassigned peptidasesunassigned-
Subfamily M10B
Name Peptidase subfamily M10B
Subfamily type peptidase M10.051 - serralysin (Serratia marcescens), MEROPS Accession MER0001096 (peptidase unit: 69-243)
Active site residues H192 E193 H196 H202 Y232 
Statistics Sequences: 1979
Identifiers: 11
Identifiers with PDB entries: 4
Other databases CATH 3.40.390.10
PFAM PF00413
SCOP 55508
Downloadable files Sequence library [FastA format]
Sequence alignment [FastA format]
Phylogenetic tree [Newick format]
Peptidases and Homologues MEROPS ID Structure
S-layer-associated peptidaseM10.035-
peptidase A (Erwinia-type)M10.052-
peptidase B (Erwinia-type)M10.053-
peptidase C (Erwinia-type)M10.054Yes
peptidase G (Erwinia-type)M10.055-
psychrophilic alkaline metallopeptidase (Pseudomonas sp.)M10.062Yes
PrtA peptidase (Photorhabdus-type)M10.063-
Subfamily M10B non-peptidase homologuesnon-peptidase homologue-
Subfamily M10B unassigned peptidasesunassigned-
Subfamily M10C
Name Peptidase subfamily M10C
Subfamily type peptidase M10.020 - fragilysin (Bacteroides fragilis), MEROPS Accession MER0001941 (peptidase unit: 236-405)
Active site residues H356 E357 H360 H366 
Statistics Sequences: 16
Identifiers: 2
Identifiers with PDB entries: 2
Other databases INTERPRO IPR001843
PFAM PF00413
Downloadable files Sequence library [FastA format]
Sequence alignment [FastA format]
Phylogenetic tree [Newick format]
Peptidases and Homologues MEROPS ID Structure
metallopeptidase II (Bacteroides fragilis)M10.039Yes
Subfamily M10C unassigned peptidasesunassigned-
Peptidases not assigned to subfamily
Peptidases and Homologues MEROPS ID Structure
Family M10 non-peptidase homologuesnon-peptidase homologue-
Family M10 unassigned peptidasesunassigned-