Biomaterial Database

The characterization of two aminopeptidase activities from the cyanobacterium Anabaena flos-aquae. 1995

G W Niven

Institute of Food Research, Reading Laboratory, UK.

Aminopeptidase activity, indicated by hydrolysis of the synthetic substrate alanine p-nitroanilide, was identified in the cyanobacterium Anabaena flos-aquae. On purification, 2 enzymes were separated by gel filtration chromatography, a 188 kDa multimer (AP-I) and a 59 kDa monomeric metalloprotein (AP-II). Their activities against a range of alanine-containing peptides were screened. Both enzymes were capable of removing a variety of N-terminal residues, including proline. Neither removed N-terminal acidic residues. The activity of AP-I appeared to be limited to di- and tri-peptides, while AP-II was capable of hydrolysing (Ala)5. It was not possible to assign the active-site chemistry of AP-I to one of the known hydrolase subgroups as none of the potential inhibitors tested had a significant inhibitory effect. This is the first reported purification of aminopeptidases from a cyanobacterium.

UI	MeSH Term	Description	Entries
D008667	Metalloproteins	Proteins that have one or more tightly bound metal ions forming part of their structure. (Dorland, 28th ed)	Metalloprotein
D011480	Protease Inhibitors	Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).	Antiprotease,Endopeptidase Inhibitor,Endopeptidase Inhibitors,Peptidase Inhibitor,Peptidase Inhibitors,Peptide Hydrolase Inhibitor,Peptide Hydrolase Inhibitors,Peptide Peptidohydrolase Inhibitor,Peptide Peptidohydrolase Inhibitors,Protease Antagonist,Protease Antagonists,Antiproteases,Protease Inhibitor,Antagonist, Protease,Antagonists, Protease,Hydrolase Inhibitor, Peptide,Hydrolase Inhibitors, Peptide,Inhibitor, Endopeptidase,Inhibitor, Peptidase,Inhibitor, Peptide Hydrolase,Inhibitor, Peptide Peptidohydrolase,Inhibitor, Protease,Inhibitors, Endopeptidase,Inhibitors, Peptidase,Inhibitors, Peptide Hydrolase,Inhibitors, Peptide Peptidohydrolase,Inhibitors, Protease,Peptidohydrolase Inhibitor, Peptide,Peptidohydrolase Inhibitors, Peptide
D011487	Protein Conformation	The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).	Conformation, Protein,Conformations, Protein,Protein Conformations
D004151	Dipeptides	Peptides composed of two amino acid units.	Dipeptide
D006868	Hydrolysis	The process of cleaving a chemical compound by the addition of a molecule of water.
D000626	Aminopeptidases	A subclass of EXOPEPTIDASES that act on the free N terminus end of a polypeptide liberating a single amino acid residue. EC 3.4.11.	Aminopeptidase
D000814	Aniline Compounds	Compounds that include the aminobenzene structure.	Phenylamine,Phenylamines,Anilines,Compounds, Aniline
D013379	Substrate Specificity	A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.	Specificities, Substrate,Specificity, Substrate,Substrate Specificities
D017033	Anabaena	A genus of CYANOBACTERIA consisting of trichomes that are untapered with conspicuous constrictions at cross-walls. A firm individual sheath is absent, but a soft covering is often present. Many species are known worldwide as major components of freshwater PLANKTON and also of many saline lakes. The species DOLICHOSPERMUM FLOS-AQUAE is responsible for acute poisonings of various animals.