BIOMAT Database Logo BIOMAT Database Logo

Primary structure of the S-peptide formed by digestion of rabbit liver fructose 1,6-biphosphatase with subtilisin. 1977

H A El-Dorry, and D K Chu, and A Dzugaj, and L H Botelho, and S Pontremoli, and B L Horecker

UI MeSH Term Description Entries
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D011817 Rabbits A burrowing plant-eating mammal with hind limbs that are longer than its fore limbs. It belongs to the family Leporidae of the order Lagomorpha, and in contrast to hares, possesses 22 instead of 24 pairs of chromosomes. Belgian Hare,New Zealand Rabbit,New Zealand Rabbits,New Zealand White Rabbit,Rabbit,Rabbit, Domestic,Chinchilla Rabbits,NZW Rabbits,New Zealand White Rabbits,Oryctolagus cuniculus,Chinchilla Rabbit,Domestic Rabbit,Domestic Rabbits,Hare, Belgian,NZW Rabbit,Rabbit, Chinchilla,Rabbit, NZW,Rabbit, New Zealand,Rabbits, Chinchilla,Rabbits, Domestic,Rabbits, NZW,Rabbits, New Zealand,Zealand Rabbit, New,Zealand Rabbits, New,cuniculus, Oryctolagus
D002268 Carboxypeptidases Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue. Carboxypeptidase
D002918 Chymotrypsin A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side. Alpha-Chymotrypsin Choay,Alphacutanée,Avazyme
D006597 Fructose-Bisphosphatase An enzyme that catalyzes the conversion of D-fructose 1,6-bisphosphate and water to D-fructose 6-phosphate and orthophosphate. EC 3.1.3.11. Fructose-1,6-Bisphosphatase,Fructose-1,6-Diphosphatase,Fructosediphosphatase,Hexosediphosphatase,D-Fructose-1,6-Bisphosphate 1-Phosphohydrolase,FDPase,Fructose-1,6-Biphosphatase,1-Phosphohydrolase, D-Fructose-1,6-Bisphosphate,D Fructose 1,6 Bisphosphate 1 Phosphohydrolase,Fructose 1,6 Biphosphatase,Fructose 1,6 Bisphosphatase,Fructose 1,6 Diphosphatase,Fructose Bisphosphatase
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
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D013381 Subtilisins A family of SERINE ENDOPEPTIDASES isolated from Bacillus subtilis. EC 3.4.21.- Alcalase,AprA-Subtilisin,Bacillus amyloliquefaciens Serine Protease,Bacillus subtilis Alkaline Proteinase,Carlsberg Subtilisin,Maxatase,Nagarse,Novo Alcalase,Profezim,Protease VII,Subtilisin 72,Subtilisin A,Subtilisin BPN',Subtilisin Carlsberg,Subtilisin DY,Subtilisin E,Subtilisin GX,Subtilisin Novo,Subtilopeptidase A,Alcalase, Novo,AprA Subtilisin,Subtilisin, Carlsberg

Related Publications

H A El-Dorry, and D K Chu, and A Dzugaj, and L H Botelho, and S Pontremoli, and B L Horecker
Ligand-induced conformational states of rabbit liver fructose 1,6-bisphosphatase as revealed by digestion with subtilisin.
May 1973, Archives of biochemistry and biophysics,
H A El-Dorry, and D K Chu, and A Dzugaj, and L H Botelho, and S Pontremoli, and B L Horecker
Structural changes of rabbit liver fructose-1,6-bisphosphatase: the effect of urea and subtilisin digestion.
June 1985, Archives of biochemistry and biophysics,
H A El-Dorry, and D K Chu, and A Dzugaj, and L H Botelho, and S Pontremoli, and B L Horecker
Fructose-1,6-biphosphatase of the small intestine. Purification and comparison with liver and muscle fructose-1,6-bisphosphatases.
August 1978, Journal of biochemistry,
H A El-Dorry, and D K Chu, and A Dzugaj, and L H Botelho, and S Pontremoli, and B L Horecker
The covalent structure of pig kidney fructose 1,6-bisphosphatase: sequence of the 60-residue NH2-terminal peptide produced by digestion with subtilisin.
July 1981, Archives of biochemistry and biophysics,
H A El-Dorry, and D K Chu, and A Dzugaj, and L H Botelho, and S Pontremoli, and B L Horecker
Rabbit liver fructose 1,6-diphosphatase. Properties of the native enzyme and their modification by subtilisin.
March 1972, Archives of biochemistry and biophysics,
H A El-Dorry, and D K Chu, and A Dzugaj, and L H Botelho, and S Pontremoli, and B L Horecker
Properties of fructose-1,6-biphosphatase of fetal and adult goat liver.
July 1987, Archiv fur experimentelle Veterinarmedizin,
H A El-Dorry, and D K Chu, and A Dzugaj, and L H Botelho, and S Pontremoli, and B L Horecker
Mutations in the yeast fructose 1,6-biphosphatase structural gene affect expression of a fructose 1,6-biphosphatase-endoglucanase A hybrid protein.
January 1993, Current genetics,
H A El-Dorry, and D K Chu, and A Dzugaj, and L H Botelho, and S Pontremoli, and B L Horecker
Modification of native sheep liver fructose-1,6-bisphosphatase by subtilisin.
May 1976, Biochemical and biophysical research communications,
H A El-Dorry, and D K Chu, and A Dzugaj, and L H Botelho, and S Pontremoli, and B L Horecker
Inhibition of rabbit liver fructose 1,6-biphosphatase by AMP: effect of temperature and physiological concentrations of cations and anions.
July 1981, Archives of biochemistry and biophysics,
H A El-Dorry, and D K Chu, and A Dzugaj, and L H Botelho, and S Pontremoli, and B L Horecker
Temporal organization of the phosphofructokinase/fructose-1,6-biphosphatase cycle.
January 1985, Advances in enzyme regulation,
Copied contents to your clipboard!