BIOMAT Database Logo BIOMAT Database Logo

Aminopeptidase PC from the hepatopancreas of the Kamchatka crab Paralithodes camtshatica. 2000

G N Rudenskaya, and A M Shmoilov, and V A Isaev, and A V Ksenofontov, and S V Shvets
School of Chemistry, Lomonosov Moscow State University, Moscow, 119899, Russia. Rudenskaya@biorg.msu.su.

Homogeneous aminopeptidase PC was isolated with yield 67% and purification degree 237 from the hepatopancreas of the Kamchatka crab Paralithodes camtshatica by ion-exchange chromatography on DEAE-Sepharose, hydrophobic chromatography on Phenyl-Sepharose, and gel-filtration on Sephadex G-150. The enzyme is a homodimer with a molecular mass 220 kD (110 x 2). Aminopeptidase PC has pI = 4.1. It hydrolyzes Leu-pNA optimally at pH 6.0 and at the optimum temperature 36-40 degrees C; in the presence of Ca2+ the enzyme is stable at pH 5.5-8.0. Aminopeptidase PC is activated by Ca2+, Mg2+, and Fe2+; it is completely inhibited by EDTA, o-phenanthroline, and bestatin. The enzyme contains four Zn atoms per molecule and is therefore a metalloaminopeptidase. The aminopeptidase PC can effectively cleave N-terminal Arg and Lys residues as well as Leu, Phe, and Met residues. Km and kcat values for hydrolysis of Leu-pNA were 0.075 mM and 0.19 sec-1 and for hydrolysis of Arg-pNA 0.078 mM and 0.48 sec-1, respectively. D-Amino acid residues cannot be cleaved. Thus, aminopeptidase PC of the Kamchatka crab has a mixed substrate specificity which is characteristic of some microbe aminopeptidases. Its N-terminal sequence ESVEIELPEGLSPLV is 46% coincident with that of yeast vacuolar aminopeptidase YSCA.

UI MeSH Term Description Entries
D008670 Metals Electropositive chemical elements characterized by ductility, malleability, luster, and conductance of heat and electricity. They can replace the hydrogen of an acid and form bases with hydroxyl radicals. (Grant & Hackh's Chemical Dictionary, 5th ed) Metal
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
D002847 Chromatography, Agarose A method of gel filtration chromatography using agarose, the non-ionic component of agar, for the separation of compounds with molecular weights up to several million. Chromatography, Sepharose,Agarose Chromatography,Sepharose Chromatography,Agarose Chromatographies,Chromatographies, Agarose,Chromatographies, Sepharose,Sepharose Chromatographies
D002850 Chromatography, Gel Chromatography on non-ionic gels without regard to the mechanism of solute discrimination. Chromatography, Exclusion,Chromatography, Gel Permeation,Chromatography, Molecular Sieve,Gel Filtration,Gel Filtration Chromatography,Chromatography, Size Exclusion,Exclusion Chromatography,Gel Chromatography,Gel Permeation Chromatography,Molecular Sieve Chromatography,Chromatography, Gel Filtration,Exclusion Chromatography, Size,Filtration Chromatography, Gel,Filtration, Gel,Sieve Chromatography, Molecular,Size Exclusion Chromatography
D002852 Chromatography, Ion Exchange Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins. Chromatography, Ion-Exchange,Ion-Exchange Chromatography,Chromatographies, Ion Exchange,Chromatographies, Ion-Exchange,Ion Exchange Chromatographies,Ion Exchange Chromatography,Ion-Exchange Chromatographies
D003386 Brachyura An infraorder of chiefly marine, largely carnivorous CRUSTACEA, in the order DECAPODA, including the genera Cancer, Uca, and Callinectes. Blue Crab,Callinectes sapidus,Carcinus maenas,Crab, Blue,Crab, Common Shore,Crab, Green,Crabs, Short-Tailed,Crabs, True,Green Crab,Uca,Common Shore Crab,European Shore Crab,Blue Crabs,Brachyuras,Carcinus maena,Common Shore Crabs,Crab, European Shore,Crab, Short-Tailed,Crab, True,Crabs, Blue,Crabs, Common Shore,Crabs, Green,Crabs, Short Tailed,Green Crabs,Shore Crab, Common,Shore Crab, European,Shore Crabs, Common,Short-Tailed Crab,Short-Tailed Crabs,True Crab,True Crabs,Ucas,maenas, Carcinus
D004064 Digestive System A group of organs stretching from the MOUTH to the ANUS, serving to breakdown foods, assimilate nutrients, and eliminate waste. In humans, the digestive system includes the GASTROINTESTINAL TRACT and the accessory glands (LIVER; BILIARY TRACT; PANCREAS). Ailmentary System,Alimentary System
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
D000596 Amino Acids Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins. Amino Acid,Acid, Amino,Acids, Amino

Related Publications

G N Rudenskaya, and A M Shmoilov, and V A Isaev, and A V Ksenofontov, and S V Shvets
[A novel endogeneous inhibitor from hepatopancreas of Kamchatka crab (Paralithodes camtschaticus)].
January 2012, Bioorganicheskaia khimiia,
G N Rudenskaya, and A M Shmoilov, and V A Isaev, and A V Ksenofontov, and S V Shvets
[Isolation of trypsin PC from the Kamchatka crab Paralithodes camtschatica and its properties].
February 1998, Bioorganicheskaia khimiia,
G N Rudenskaya, and A M Shmoilov, and V A Isaev, and A V Ksenofontov, and S V Shvets
[Isolation and properties of carboxypeptidase from the Kamchatka crab Paralithodes camtshatica].
April 1995, Bioorganicheskaia khimiia,
G N Rudenskaya, and A M Shmoilov, and V A Isaev, and A V Ksenofontov, and S V Shvets
[Ribonuclease from the hepatopancreas of the red king crab Paralithodes camtschatica].
January 2009, Prikladnaia biokhimiia i mikrobiologiia,
G N Rudenskaya, and A M Shmoilov, and V A Isaev, and A V Ksenofontov, and S V Shvets
[Isolation and properties of serine proteinase PC from the Kamchatka crab, Paralithodes camtschatica--a proteolytic enzyme with broad specificity].
June 1996, Biokhimiia (Moscow, Russia),
G N Rudenskaya, and A M Shmoilov, and V A Isaev, and A V Ksenofontov, and S V Shvets
[Chitosan depolymerization by enzymes from hepatopancreas of the crab Paralithodes camtschaticus].
January 2003, Prikladnaia biokhimiia i mikrobiologiia,
G N Rudenskaya, and A M Shmoilov, and V A Isaev, and A V Ksenofontov, and S V Shvets
[Phosphatases and phosphodiesterases isolated from the red king crab (Paralithodes camtschatica) hepatopancreas].
January 2008, Prikladnaia biokhimiia i mikrobiologiia,
G N Rudenskaya, and A M Shmoilov, and V A Isaev, and A V Ksenofontov, and S V Shvets
[Glycolytic activity of enzyme preparation from the red king crab (Paralithodes camtschaticus) hepatopancreas].
January 2008, Prikladnaia biokhimiia i mikrobiologiia,
G N Rudenskaya, and A M Shmoilov, and V A Isaev, and A V Ksenofontov, and S V Shvets
[Properties of chitinolytic enzymes from the hepatopancreas of the red king crab (Paralithodes camtschaticus)].
January 2007, Prikladnaia biokhimiia i mikrobiologiia,
G N Rudenskaya, and A M Shmoilov, and V A Isaev, and A V Ksenofontov, and S V Shvets
[Collagenolytic protease complex from the Kamchatka crab hepatopancreas: separation of the individual components].
September 1999, Biulleten' eksperimental'noi biologii i meditsiny,
Copied contents to your clipboard!