Metalloproteases

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Metalloproteases (formerly: metallopeptidases) are enzymes , the peptide bonds of a protein ( protein ) can cleave ( proteolysis ), in which one molecule of water is consumed ( hydrolysis ) and the water molecule of one or two metal cations is maintained in position. The metal ion is bound to amino acid side residues belonging to the enzyme .

Classification

A first rough classification of metalloproteases can be done according to the type of proteolysis, into metallo endopeptidases (metalloproteinases) and metallo exopeptidases (metallopeptidases in the narrower / newer sense).

Classification according to UniProt / MEROPS

The UniProt Consortium regularly publishes a list of peptidases that categorize these enzymes according to their evolutionary origin. The data in the list are provided with high-quality information and can be called up in the MEROPS database. Closely related molecules are grouped together in families whose identifiers consist of a letter ('M' for metalloproteases) and a number. Families, in turn, belong to clans whose families are related. Clan identifiers have a letter instead of numbers.

There are 54 metalloprotease families in 15 clans (as of 2008), with clan MA with 39 families being of outstanding importance. 19 of these 39 families alone can be assigned to the neutral zinc metallopeptidases.

clan designation Exo Endo metal Exemplary enzyme UniProt Familys
MA Neutral zinc metallopeptidases zinc Thermolysin ( Bacillus stearothermophilus ) P06874 M1-13 M26-7 M30 M32 M34-6 M41 M43 M48 M54 M56-7 M60-1 M64 M66 M72
MC Zinc carboxypeptidases Exo zinc Carboxypeptidase  A1 ( Bos taurus ) P00730 M14
MD Exo zinc D-Ala-D-Ala-carboxypeptidase ( Streptomyces albus ) P00733 M15 M74
ME Insulinases Endo zinc Pitrilysin ( E. coli ) P05458 M16 M44
MF Cytosolic aminopeptidases Exo Zinc, manganese Leucine aminopeptidase ( Bos taurus ) P00727 M17
MG Methionine aminopeptidases Exo Zinc / cobalt Methionine aminopeptidase ( Salmonella typhimurium ) P0A1X6 M24
MH Exo 2 zinc Bacterial leucine aminopeptidase ( Vibrio proteolyticus ) Q01693 M18 M20 M28 M42
MJ Renal dipeptidases Exo 2 zinc Isoaspartyl dipeptidase ( E. coli K12) P39377 M19 M38
MK Glycoproteases Endo (2 zinc) Glycoprotease ( Mannheimia typhimurium ) P36175 M22
MM Neutral zinc metallopeptidases Endo zinc Site-2 protease ( Homo sapiens ) O43462 M50
MN Exo 2 zinc D- aminoprotease ( Bacillus subtilis ) P26902 M55
MO Endo zinc Lysostaphin ( Staphylococcus simulans ) P10547 M23
MP zinc JAMM-like protein (Archaea) A0B7A7 M67
MQ 2 · cobalt Aminopeptidase T ( Thermus aquaticus ) P23341 M29
M- (not assigned) M49 M73 M75-6

Examples

The following are the main human metalloproteases:

Matrix metalloproteinases

Matrix metalloproteases are a special type of metalloproteases . They can be divided into

In the MEROPS system, matrix metalloproteases are completely contained in the M10A family.

ADAM metalloproteases

In 2006, researchers at Johannes Gutenberg University Mainz published the results of experiments in which it was shown in mice that the plaques that are formed in Alzheimer's disease can be broken down by a certain metalloprotease. The ADAM metalloproteases ADAM10 , a so-called α-secretase , can prevent the formation of such β-amyloid deposits in the brain. It is a metalloprotease that is active in the synapses of healthy nerve cells.

ADAM metalloproteases completely belong to the MEROPS family M12.

Further examples

Important metalloproteases of other living things:

Individual evidence

  1. ^ Definition of metallopeptidase activity at GeneOntology
  2. ↑ UniProt: Peptidase families: classification and list of entries.
  3. ↑ MEROPS: List of clans and families
  4. ^ Hannes Leischner: Basics oncology. Elsevier GmbH Germany, 2007. ISBN 3437423266 , p. 10
  5. ↑ U. Schmitt et al .: Over-expression of two different forms of the a-secretase ADAM10 affects learning and memory in mice. Behav Brain Res. 175/2/ 2006 . Pp. 278-284. PMID 17014917

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