Metalloexopeptidase - Misplaced Pages

Type of enzyme

This article has multiple issues. Please help improve it or discuss these issues on the talk page. (Learn how and when to remove these messages)

This article needs additional citations for verification. Please help improve this article by adding citations to reliable sources. Unsourced material may be challenged and removed.
Find sources: "Metalloexopeptidase" – news · newspapers · books · scholar · JSTOR (May 2016) (Learn how and when to remove this message)

This article may be too technical for most readers to understand. Please help improve it to make it understandable to non-experts, without removing the technical details. (May 2016) (Learn how and when to remove this message)

(Learn how and when to remove this message)

A metalloexopeptidase is a type of enzyme that acts as a metalloproteinase exopeptidase. These enzymes have a catalytic mechanism involving a metal, often zinc. They function in molecular biology 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 (or dipeptide) for use.

Metallocarboxypeptidase

The terms "metallo carboxypeptidase", "metallo-carboxypeptidase" and "metallocarboxypeptidase" are used to describe a metalloexopeptidase carboxypeptidase. These peptidases specifically target the C-terminus, the unbound carboxyl group (-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 (EC number) system, metallocarboxypeptidases fall under EC 3.4.17. Examples of these compounds in the human genome 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 pairs (bases) while the latter resides in Chromosome 11 and is made up of 56,221 bases.

References

"ENZYME: 3.4.17.-". enzyme.expasy.org. Retrieved 2016-05-21.
"AGBL1". www.genecards.org. Retrieved 2016-05-21.
"AGBL2". www.genecards.org. Retrieved 2016-05-21.

External links

Metalloexopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

Hydrolase: proteases (EC 3.4)

3.4.11-19: Exopeptidase

3.4.11	Aminopeptidase Alanine Arginyl Aspartyl Cystinyl Leucyl Glutamyl Methionyl 1 2 O
3.4.13	Dipeptidase 1 2 3
3.4.14	Dipeptidyl peptidase Cathepsin C Dipeptidyl peptidase-4 Tripeptidyl peptidase Tripeptidyl peptidase I Tripeptidyl peptidase II
3.4.15	Angiotensin-converting enzyme
3.4.16	Serine type carboxypeptidases: Cathepsin A DD-Transpeptidase
3.4.17	Metalloexopeptidases Carboxypeptidase A A2 B C E Glutamate II
Other/ungrouped	Metalloexopeptidase

3.4.21-25: Endopeptidase

Other/ungrouped: Amyloid precursor protein secretase

3.4.99: Unknown

Staphylokinase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Portal:

Biology

This enzyme-related article is a stub. You can help Misplaced Pages by expanding it.

Categories:

Metallocarboxypeptidase

Enzyme Commission number

See also

References

External links