Biomaterial Database

Characterization and primary specificity of an extracellular metalloproteinase from Serratia marcescens. 1994

N Kim, and S I Kim

Food Chemistry and Physics Division, Korea Food Research Institute, Bundang-ku, Songnam-si, Kyonggi-do.

An extracellular endopeptidase (proteinase) from Serratia marcescens (Serratia marcescens extracellular proteinase, EC 3.4.24.4), purified to homogeneity, was analyzed for enzyme properties. The enzyme has a polypeptide chain molecular mass of 52 kDa as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The enzyme has an optimal temperature of 40 degrees C and an optimal pH of 7.0. Enzyme activity was enhanced over two times by the addition of Ca2+ and Mg2+ ions and eliminated almost completely by the presence of 0.2% SDS. The enzyme has broad substrate specificity and contains neither cysteine nor methionine. Low homology was found between the NH2-terminal amino acid sequence of the enzyme of this study and the NH2-terminal sequence of a proteinase from another strain of S. marcescens. Chemical modification with N-bromosuccinimide, 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide, and 8-anilino-1-naphthalene sulfonic acid and by photooxidation with methylene blue reduced enzyme activity considerably. The enzyme was shown to have broad peptide bond specificity judging from the contribution of 11 amino acids to the carboxyl side of the peptide bonds hydrolyzed.

UI	MeSH Term	Description	Entries
D008666	Metalloendopeptidases	ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.	Metallo-Endoproteinases,Metalloendopeptidase
D008969	Molecular Sequence Data	Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.	Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D008970	Molecular Weight	The sum of the weight of all the atoms in a molecule.	Molecular Weights,Weight, Molecular,Weights, Molecular
D005110	Extracellular Space	Interstitial space between cells, occupied by INTERSTITIAL FLUID as well as amorphous and fibrous substances. For organisms with a CELL WALL, the extracellular space includes everything outside of the CELL MEMBRANE including the PERIPLASM and the cell wall.	Intercellular Space,Extracellular Spaces,Intercellular Spaces,Space, Extracellular,Space, Intercellular,Spaces, Extracellular,Spaces, Intercellular
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001426	Bacterial Proteins	Proteins found in any species of bacterium.	Bacterial Gene Products,Bacterial Gene Proteins,Gene Products, Bacterial,Bacterial Gene Product,Bacterial Gene Protein,Bacterial Protein,Gene Product, Bacterial,Gene Protein, Bacterial,Gene Proteins, Bacterial,Protein, Bacterial,Proteins, Bacterial
D012706	Serratia marcescens	A species of gram-negative, facultatively anaerobic, rod-shaped bacteria found in soil, water, food, and clinical specimens. It is a prominent opportunistic pathogen for hospitalized patients.
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