A metalloexopeptidase is a type of
enzyme
An enzyme () is a protein that acts as a biological catalyst by accelerating chemical reactions. The molecules upon which enzymes may act are called substrate (chemistry), substrates, and the enzyme converts the substrates into different mol ...
that acts as a
metalloproteinase exopeptidase
An exopeptidase is any peptidase that catalyzes the cleavage of the terminal (or the penultimate) peptide bond; the process releases a single amino acid, dipeptide or a tripeptide from the peptide chain. Depending on whether the amino acid is r ...
.
These enzymes have a
catalytic mechanism involving a
metal
A metal () is a material that, when polished or fractured, shows a lustrous appearance, and conducts electrical resistivity and conductivity, electricity and thermal conductivity, heat relatively well. These properties are all associated wit ...
, often
zinc
Zinc is a chemical element; it has symbol Zn and atomic number 30. It is a slightly brittle metal at room temperature and has a shiny-greyish appearance when oxidation is removed. It is the first element in group 12 (IIB) of the periodic tabl ...
. They function in
molecular biology
Molecular biology is a branch of biology that seeks to understand the molecule, molecular basis of biological activity in and between Cell (biology), cells, including biomolecule, biomolecular synthesis, modification, mechanisms, and interactio ...
as agents that cut the terminal (or penultimate)
peptide bonds ending peptide chains. Analogous to slicing the end off a loaf of bread, the process releases a single
amino acid
Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. Only these 22 a ...
(or dipeptide) for use.
Metallocarboxypeptidase
The terms "metallo carboxypeptidase", "metallo-carboxypeptidase" and "metallocarboxypeptidase" are used to describe a metalloexopeptidase
carboxypeptidase
A carboxypeptidase ( EC number 3.4.16 - 3.4.18) is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal (C-terminal) end of a protein or peptide. This is in contrast to an aminopeptidases, which cleave peptide b ...
. These peptidases specifically target the
C-terminus
The C-terminus (also known as the carboxyl-terminus, carboxy-terminus, C-terminal tail, carboxy tail, C-terminal end, or COOH-terminus) is the end of an amino acid chain (protein
Proteins are large biomolecules and macromolecules that comp ...
, the unbound
carboxyl group
In organic chemistry, a carboxylic acid is an organic acid that contains a carboxyl group () attached to an R-group. The general formula of a carboxylic acid is often written as or , sometimes as with R referring to an organyl group (e.g. ...
(-COOH) at one distinct end of the amino acid chain (cutting one side from a loaf of bread rather than the end).
Enzyme Commission number
Using the
Enzyme Commission number
The Enzyme Commission number (EC number) is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. As a system of enzyme nomenclature, every EC number is associated with a recommended name for the correspon ...
(EC number) system, metallocarboxypeptidases fall under
EC 3.4.17
EC or ec may refer to:
Arts and entertainment
* EC Comics, an American publisher of comic books
* '' Electric Circus'', a Canadian television program
* Eric Clapton Stratocaster, signature model guitars by Fender
Businesses and organisations Go ...
. Examples of these compounds in the
human genome
The human genome is a complete set of nucleic acid sequences for humans, encoded as the DNA within each of the 23 distinct chromosomes in the cell nucleus. A small DNA molecule is found within individual Mitochondrial DNA, mitochondria. These ar ...
include AGBL1 and AGBL2, known also as ATP/GTP Binding Protein-Like 1 and 2, respectively. The former resides in
Chromosome 15 and is made up of 951,392
base pair
A base pair (bp) is a fundamental unit of double-stranded nucleic acids consisting of two nucleobases bound to each other by hydrogen bonds. They form the building blocks of the DNA double helix and contribute to the folded structure of both DNA ...
s (bases) while the latter resides in
Chromosome 11 and is made up of 56,221 bases.
See also
*
Enzyme catalysis
Enzyme catalysis is the increase in the rate of a process by an "enzyme", a biological molecule. Most enzymes are proteins, and most such processes are chemical reactions. Within the enzyme, generally catalysis occurs at a localized site, calle ...
*
Hydrolase
In biochemistry, hydrolases constitute a class of enzymes that commonly function as biochemical catalysts that use water to break a chemical bond:
:\ce \quad \xrightarrowtext\quad \ce
This typically results in dividing a larger molecule into s ...
References
External links
*
EC 3.4.17
{{enzyme-stub