Citrinin hydrate inhibits serotonin N-acetyltransferase catalyzing the conversion of serotonin to N-acetylserotonin

In Kyoung Lee; Bong Sik Yun; Kyong Tai Kim; Bo Hwa Choi; Tae Ju Park; Young Ho Kim; Ick Dong Yoo

Citrinin hydrate inhibits serotonin N-acetyltransferase catalyzing the conversion of serotonin to N-acetylserotonin

In Kyoung Lee
, Bong Sik Yun
, Kyong Tai Kim
, Bo Hwa Choi
, Tae Ju Park
, Young Ho Kim
, Ick Dong Yoo^*

^*Corresponding author for this work

Environmental Biotechnology

Korea Research Institute of Bioscience and Biotechnology

Research output: Contribution to journal › Journal article › peer-review

1 Scopus citations

Abstract

In an attempt to search for serotonin N-acetyltransferase (arylalkylamine N-acetyltransferase, AA-NAT) inhibitors from microbial metabolites, we found the culture broth of Penicillium sp. 80722 which showed a strong inhibitory activity against AA-NAT. The active principle has been identified as citrinin hydrate through bioassay-guided fractionation of cultural broth, and structure elucidation derived by spectroscopic analyses. Citrinin hydrate inhibits AA-NAT with an IC₅₀ value of 173 μM in a dose-dependent manner. Although citrinin hydrate was previously isolated as human rhinovirus 3C-protease inhibitor, this was recognized as the first AA-NAT inhibitor isolated from natural sources.

Original language	English
Pages (from-to)	1099-1101
Number of pages	3
Journal	Journal of Microbiology and Biotechnology
Volume	11
Issue number	6
State	Published - 2001

Keywords

Citrinin hydrate
Penicillium sp.
Serotonin N-acetyltransferase (AA-NAT) inhibitor

Cite this

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title = "Citrinin hydrate inhibits serotonin N-acetyltransferase catalyzing the conversion of serotonin to N-acetylserotonin",

abstract = "In an attempt to search for serotonin N-acetyltransferase (arylalkylamine N-acetyltransferase, AA-NAT) inhibitors from microbial metabolites, we found the culture broth of Penicillium sp. 80722 which showed a strong inhibitory activity against AA-NAT. The active principle has been identified as citrinin hydrate through bioassay-guided fractionation of cultural broth, and structure elucidation derived by spectroscopic analyses. Citrinin hydrate inhibits AA-NAT with an IC50 value of 173 μM in a dose-dependent manner. Although citrinin hydrate was previously isolated as human rhinovirus 3C-protease inhibitor, this was recognized as the first AA-NAT inhibitor isolated from natural sources.",

keywords = "Citrinin hydrate, Penicillium sp., Serotonin N-acetyltransferase (AA-NAT) inhibitor",

author = "Lee, \{In Kyoung\} and Yun, \{Bong Sik\} and Kim, \{Kyong Tai\} and Choi, \{Bo Hwa\} and Park, \{Tae Ju\} and Kim, \{Young Ho\} and Yoo, \{Ick Dong\}",

year = "2001",

language = "English",

volume = "11",

pages = "1099--1101",

journal = "Journal of Microbiology and Biotechnology",

issn = "1017-7825",

number = "6",

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TY - JOUR

T1 - Citrinin hydrate inhibits serotonin N-acetyltransferase catalyzing the conversion of serotonin to N-acetylserotonin

AU - Lee, In Kyoung

AU - Yun, Bong Sik

AU - Kim, Kyong Tai

AU - Choi, Bo Hwa

AU - Park, Tae Ju

AU - Kim, Young Ho

AU - Yoo, Ick Dong

PY - 2001

Y1 - 2001

N2 - In an attempt to search for serotonin N-acetyltransferase (arylalkylamine N-acetyltransferase, AA-NAT) inhibitors from microbial metabolites, we found the culture broth of Penicillium sp. 80722 which showed a strong inhibitory activity against AA-NAT. The active principle has been identified as citrinin hydrate through bioassay-guided fractionation of cultural broth, and structure elucidation derived by spectroscopic analyses. Citrinin hydrate inhibits AA-NAT with an IC50 value of 173 μM in a dose-dependent manner. Although citrinin hydrate was previously isolated as human rhinovirus 3C-protease inhibitor, this was recognized as the first AA-NAT inhibitor isolated from natural sources.

AB - In an attempt to search for serotonin N-acetyltransferase (arylalkylamine N-acetyltransferase, AA-NAT) inhibitors from microbial metabolites, we found the culture broth of Penicillium sp. 80722 which showed a strong inhibitory activity against AA-NAT. The active principle has been identified as citrinin hydrate through bioassay-guided fractionation of cultural broth, and structure elucidation derived by spectroscopic analyses. Citrinin hydrate inhibits AA-NAT with an IC50 value of 173 μM in a dose-dependent manner. Although citrinin hydrate was previously isolated as human rhinovirus 3C-protease inhibitor, this was recognized as the first AA-NAT inhibitor isolated from natural sources.

KW - Citrinin hydrate

KW - Penicillium sp.

KW - Serotonin N-acetyltransferase (AA-NAT) inhibitor

UR - https://www.scopus.com/pages/publications/0035695128

M3 - Journal article

AN - SCOPUS:0035695128

SN - 1017-7825

VL - 11

SP - 1099

EP - 1101

JO - Journal of Microbiology and Biotechnology

JF - Journal of Microbiology and Biotechnology

IS - 6

ER -

Citrinin hydrate inhibits serotonin N-acetyltransferase catalyzing the conversion of serotonin to N-acetylserotonin

Abstract

Keywords

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