Clostridial aminopeptidase (, ''Clostridium histolyticum aminopeptidase'') is an

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 ...

. This enzyme catalyses the following

chemical reaction A chemical reaction is a process that leads to the chemistry, chemical transformation of one set of chemical substances to another. When chemical reactions occur, the atoms are rearranged and the reaction is accompanied by an Gibbs free energy, ...

: Release of any N-terminal

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 ...

, including

proline Proline (symbol Pro or P) is an organic acid classed as a proteinogenic amino acid (used in the biosynthesis of proteins), although it does not contain the amino group but is rather a secondary amine. The secondary amine nitrogen is in the p ...

and

hydroxyproline (2''S'',4''R'')-4-Hydroxyproline, or L-hydroxyproline ( C5 H9 O3 N), is an amino acid, abbreviated as Hyp or O, ''e.g.'', in Protein Data Bank. Structure and discovery In 1902, Hermann Emil Fischer isolated hydroxyproline from hydrolyzed gela ...

, but no cleavage of Xaa-Pro- This enzyme is secreted enzyme from ''

Clostridium histolyticum ''Hathewaya histolytica'' (formerly ''Clostridium histolyticum'') is a species of bacteria found in feces and the soil. It is a motile, gram-positive, aerotolerant anaerobe. ''H. histolytica'' is pathogenic in many species, including guinea pigs ...

''. It requiring Mn²⁺ or Co²⁺.

References

External links

* {{Portal bar, Biology, border=no EC 3.4.11