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Titolo:
PURIFICATION AND PROPERTIES OF AN INTRACELLULAR LEUCINE AMINOPEPTIDASE FROM THE FUNGUS, PENICILLIUM-CITRINUM STRAIN IFO-6352
Autore:
KWON SC; PARK SJ; CHO JM;
Indirizzi:
BIOTECH RES INST,LG CHEM RES PK,POB 61 TAEJON 305600 SOUTH KOREA BIOTECH RES INST TAEJON 305600 SOUTH KOREA
Titolo Testata:
Journal of industrial microbiology
fascicolo: 1, volume: 17, anno: 1996,
pagine: 30 - 35
SICI:
0169-4146(1996)17:1<30:PAPOAI>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
STREPTOMYCES-GRISEUS AMINOPEPTIDASE; BOVINE LENS; METHIONINE AMINOPEPTIDASE; SACCHAROMYCES-CEREVISIAE; BINDING; ENZYME; MODULATION; MECHANISM; PROTEIN; GENE;
Keywords:
LEUCINE AMINOPEPTIDASE; PENICILLIUM CITRINUM; METHIONINE REMOVAL;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
25
Recensione:
Indirizzi per estratti:
Citazione:
S.C. Kwon et al., "PURIFICATION AND PROPERTIES OF AN INTRACELLULAR LEUCINE AMINOPEPTIDASE FROM THE FUNGUS, PENICILLIUM-CITRINUM STRAIN IFO-6352", Journal of industrial microbiology, 17(1), 1996, pp. 30-35

Abstract

An intracellular leucine aminopeptidase (LAP) from Penicillium citrinum (IFO 6352) was purified to homogeneity using three successive purification steps. The enzyme has a native molecular mass of 63 kDa using HPLC gel filtration analysis and a molecular mass of 65 kDa when usingSDS-polyacrylamide gel electrophoresis. This monomeric aminopeptidaseshowed maximum enzyme activity at pH 8.5. An optimum temperature was 45-50 degrees C when L-Leu-p-nitroanilide (pNA) was the substrate, andenzyme activity drastically decreased above 60 degrees C. The Michaelis-Menten constants for L-Leu-pNA and L-Met-pNA were 2.7 mM and 1.8 mM, respectively. When the enzyme reacted with biosynthetic methionyl human growth hormone, it showed high specificity for N-terminal methionine residue and recognized a stop sequence (Xaa-Pro). The aminopeptidase was inactivated by EDTA or 1,10-phenanthroline, indicating that it is a metallo-exoprotease. Enzyme activity was restored to 90% of maximal activity by addition of Co2+ ions. The activity of EDTA-treated enzyme was restored by addition of Zn2+, but reconstitution with Ca2+, Mg2 or Mn2+ restored some enzyme activity. It is likely that Co2+ ions play an important role in the catalysis or stability of the Penicilliumcitrinum aminopeptidase, as zinc plays a similar function in other leucine aminopeptidases.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 04:30:36