Epostatin, new inhibitor of dipeptidyl peptidase II, produced by Streptomyces sp. MJ995-OF5. I. Taxonomy of producing strain, fermentation, isolation, physico-chemical properties and biological properties.
A new inhibitor of dipeptidyl peptidase II (DPP-II, EC 3.4.14.2), designated as epostatin, was discovered in the fermentation broth of a strain isolated in our institute. The strain has been identified as Streptomyces sp. MJ995-OF5 on the basis of taxonomic studies. Epostatin was obtained as a yellow powder after seqential purification by chromatography on Diaion HP-20, n-butanol extraction, Sephadex LH-20 column chromatography and centrifugal partition chromatography (CPC). Epostatin inhibited DPP-II competitively in a dose dependent manner. The compound was slightly inhibitory against other dipeptidyl peptidases.
Akiyama
T
T
Institute of Microbial Chemistry, Tokyo, Japan.
Harada
S
S
Kojima
F
F
Kinoshita
N
N
Hamada
M
M
Muraoka
Y
Y
Aoyagi
T
T
Takeuchi
T
T
D000409:Alanine / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D000577:Amides / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000037:antagonists & inhibitors*; D004988:Ethers, Cyclic / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D005285:Fermentation; D015842:Serine Proteinase Inhibitors / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D013302:Streptomyces / Q000145:classification* / Q000378:metabolism
D000577:Amides; D004988:Ethers, Cyclic; D015842:Serine Proteinase Inhibitors; C112180:epostatin; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; C100151:dipeptidyl peptidase II; D000409:Alanine