Newly discovered penicillin acylase activity of aculeacin A acylase from Actinoplanes utahensis

Jesús Torres-Bacete; Daniel Hormigo; Maribel Stuart; Miguel Arroyo; Pedro Torres; María P. Castillón; Carmen Acebal; José L. García; Isabel De La Mata

doi:10.1128/AEM.00452-07

Newly discovered penicillin acylase activity of aculeacin A acylase from Actinoplanes utahensis

Jesús Torres-Bacete, Daniel Hormigo, Maribel Stuart, Miguel Arroyo, Pedro Torres, María P. Castillón, Carmen Acebal, José L. García, Isabel De La Mata

Cancer Signaling and Microenvironment (CSM)

Research output: Contribution to journal › Article › peer-review

20 Scopus citations

Abstract

Aculeacin A acylase from Actinoplanes utahensis produced by Streptomyces lividans revealed acylase activities that are able to hydrolyze penicillin V and several natural aliphatic penicillins. Penicillin K was the best substrate, showing a catalytic efficiency of 34.79 mM^-1 s^-1. Furthermore, aculeacin A acylase was highly thermostable, with a midpoint transition temperature of 81.5°C.

Original language	English
Pages (from-to)	5378-5381
Number of pages	4
Journal	Applied and Environmental Microbiology
Volume	73
Issue number	16
DOIs	https://doi.org/10.1128/AEM.00452-07
State	Published - Aug 2007

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title = "Newly discovered penicillin acylase activity of aculeacin A acylase from Actinoplanes utahensis",

abstract = "Aculeacin A acylase from Actinoplanes utahensis produced by Streptomyces lividans revealed acylase activities that are able to hydrolyze penicillin V and several natural aliphatic penicillins. Penicillin K was the best substrate, showing a catalytic efficiency of 34.79 mM-1 s-1. Furthermore, aculeacin A acylase was highly thermostable, with a midpoint transition temperature of 81.5°C.",

author = "Jes{\'u}s Torres-Bacete and Daniel Hormigo and Maribel Stuart and Miguel Arroyo and Pedro Torres and Castill{\'o}n, \{Mar{\'i}a P.\} and Carmen Acebal and Garc{\'i}a, \{Jos{\'e} L.\} and \{De La Mata\}, Isabel",

year = "2007",

month = aug,

doi = "10.1128/AEM.00452-07",

language = "English",

volume = "73",

pages = "5378--5381",

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T1 - Newly discovered penicillin acylase activity of aculeacin A acylase from Actinoplanes utahensis

AU - Torres-Bacete, Jesús

AU - Hormigo, Daniel

AU - Stuart, Maribel

AU - Arroyo, Miguel

AU - Torres, Pedro

AU - Castillón, María P.

AU - Acebal, Carmen

AU - García, José L.

AU - De La Mata, Isabel

PY - 2007/8

Y1 - 2007/8

N2 - Aculeacin A acylase from Actinoplanes utahensis produced by Streptomyces lividans revealed acylase activities that are able to hydrolyze penicillin V and several natural aliphatic penicillins. Penicillin K was the best substrate, showing a catalytic efficiency of 34.79 mM-1 s-1. Furthermore, aculeacin A acylase was highly thermostable, with a midpoint transition temperature of 81.5°C.

AB - Aculeacin A acylase from Actinoplanes utahensis produced by Streptomyces lividans revealed acylase activities that are able to hydrolyze penicillin V and several natural aliphatic penicillins. Penicillin K was the best substrate, showing a catalytic efficiency of 34.79 mM-1 s-1. Furthermore, aculeacin A acylase was highly thermostable, with a midpoint transition temperature of 81.5°C.

UR - https://www.scopus.com/pages/publications/34548291927

U2 - 10.1128/AEM.00452-07

DO - 10.1128/AEM.00452-07

M3 - Article

C2 - 17586674

SN - 0099-2240

VL - 73

SP - 5378

EP - 5381

JO - Applied and Environmental Microbiology

JF - Applied and Environmental Microbiology

IS - 16

ER -

Newly discovered penicillin acylase activity of aculeacin A acylase from Actinoplanes utahensis

Abstract

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