SYNTHESIS OF ENTEROSTATIN-AMIDE BY THE XAA-PROLYL DIPEPTIDYL AMINOPEPTIDASE FROM LACTOCOCCUS-LACTIS SUBSP LACTIS NCDO-763

被引：0

作者：

HOUBART, V ^{[1
]}

RIBADEAUDUMAS, B ^{[1
]}

CHICH, JF ^{[1
]}

机构：

[1] INRA,UNITE PROT,RECH LAITIERES STN,F-78352 JOUY EN JOSAS,FRANCE

来源：

BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY | 1995年 / 21卷

关键词：

D O I：

暂无

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The Xaa-prolyl dipeptidyl aminopeptidase from Lactococcus lactis. subsp. lactis N.C.D.O. 763 (PepX; 'X-PDAP'; EC 3.4.14.5) was used as a catalyst in the kinetically controlled synthesis of enterostatin-amide, APGPR-NH2 (the one-letter code for amino acids is used). Two successive reactions in aqueous media were performed to obtain this peptide from R-NH2, GP and AP p-nitroanilide. The reaction conditions were optimized by varing the pH and nucleophile concentration. The first reaction gave GPR-NH2, the amide of the fibrin anti-polymerant GPR with a 90% yield. The second reaction produced APGPR-NH2, with a 49.5% yield. The overall yield of both reactions was 45%. The reaction time was similar to 30 min for each step.

引用

页码：149 / 159

页数：11

共 33 条

[21] PURIFICATION AND CHARACTERIZATION OF AN AMINOPEPTIDASE FROM LACTOCOCCUS-LACTIS SUBSP CREMORIS WG2
TAN, PST
KONINGS, WN
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1990, 56 (02) : 526 - 532
[22] PURIFICATION, CRYSTALLIZATION, AND PRELIMINARY-X-RAY ANALYSIS OF PEPX, AN X-PROLYL DIPEPTIDYL AMINOPEPTIDASE FROM LACTOCOCCUS-LACTIS
CHICH, JF
RIGOLET, P
NARDI, M
GRIPON, JC
RIBADEAUDUMAS, B
BRUNIE, S
PROTEINS-STRUCTURE FUNCTION AND GENETICS, 1995, 23 (02): : 278 - 281
[23] Improvement of fermentation conditions for the production of X-prolyl-dipeptidyl aminopeptidase from Lactococcus lactis
Pérez-Guzmán, AE
Victoria, TCY
Cruz-Camarillo, R
Hernández-Sánchez, H
WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY, 2004, 20 (04): : 413 - 417
[24] The structural basis for catalysis and specificity of the X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis
Rigolet, P
Mechin, I
Delage, MM
Chich, JF
STRUCTURE, 2002, 10 (10) : 1383 - 1394
[25] Improvement of Fermentation Conditions for the Production of X-Prolyl-Dipeptidyl Aminopeptidase from Lactococcus Lactis
Alfredo E. Pérez-Guzmán
Teresa Cruz y Victoria
Ramón Cruz-Camarillo
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World Journal of Microbiology and Biotechnology, 2004, 20 : 413 - 417
[26] Characterization and role of the branched-chain aminotransferase (BcaT) isolated from Lactococcus lactis subsp cremoris NCDO 763
Yvon, M
Chambellon, E
Bolotin, A
Roudot-Algaron, F
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2000, 66 (02) : 571 - 577
[27] EFFECT OF PEPTIDES FROM THE SEQUENCE-58-72 OF BETA-CASEIN ON THE ACTIVITY OF ENDOPEPTIDASE, AMINOPEPTIDASE, AND X-PROLYL-DIPEPTIDYL AMINOPEPTIDASE FROM LACTOCOCCUS-LACTIS SSP LACTIS MG1363
STEPANIAK, L
FOX, PF
SORHAUG, T
GRABSKA, J
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1995, 43 (03) : 849 - 853
[28] Statistical optimization of cell disruption techniques for releasing intracellular X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis spp. lactis
Ustun-Aytekin, Ozlem
Ansoy, Sevda
Aytekin, Ali Ozhan
Yildiz, Ece
ULTRASONICS SONOCHEMISTRY, 2016, 29 : 163 - 171
[29] CLONING, NUCLEOTIDE-SEQUENCE AND EXPRESSION IN STREPTOMYCES-LIVIDANS AND ESCHERICHIA-COLI OF PABB FROM LACTOCOCCUS-LACTIS SUBSP LACTIS NCDO-496
ARHIN, FF
VINING, LC
JOURNAL OF GENERAL MICROBIOLOGY, 1993, 139 : 1785 - 1793
[30] CLONING AND SEQUENCING OF PEPC, A CYSTEINE AMINOPEPTIDASE GENE FROM LACTOCOCCUS-LACTIS SUBSP CREMORIS AM2
CHAPOTCHARTIER, MP
NARDI, M
CHOPIN, MC
CHOPIN, A
GRIPON, JC
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1993, 59 (01) : 330 - 333

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