Biochemical characterization of SFC-1, a class A carbapenem-hydrolyzing β-lactamase

Fátima Fonseca; Ana Cristina Sarmento; Isabel Henriques; Bart Samyn; Jozef Van Beeumen; Pedro Domingues; Maria Rosário Domingues; Maria José Saavedra; António Correia

doi:10.1128/AAC.00491-07

Biochemical characterization of SFC-1, a class A carbapenem-hydrolyzing β-lactamase

Fátima Fonseca
, Ana Cristina Sarmento
, Isabel Henriques
, Bart Samyn
, Jozef Van Beeumen
, Pedro Domingues
, Maria Rosário Domingues
, Maria José Saavedra
, António Correia^*

^*Corresponding author for this work

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

25 Citations (Scopus)

Abstract

The carbapenem-hydrolyzing β-lactamase SFC-1 from Serratia fonticola UTAD54 was overexpressed in Escherichia coli, purified, and characterized. The enzyme exhibited an apparent molecular mass of 30.5 kDa, determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. SFC-1 hydrolyzes penicillins, cephalosporins, aztreonam, and carbapenems and is inhibited by clavulanic acid, sulbactam, and tazobactam.

Original language	English
Pages (from-to)	4512-4514
Number of pages	3
Journal	Antimicrobial Agents and Chemotherapy
Volume	51
Issue number	12
DOIs	https://doi.org/10.1128/AAC.00491-07
Publication status	Published - Dec 2007
Externally published	Yes

Access to Document

10.1128/AAC.00491-07

Cite this

@article{a5554157eae94e4a80d1e1291ca12914,

title = "Biochemical characterization of SFC-1, a class A carbapenem-hydrolyzing β-lactamase",

abstract = "The carbapenem-hydrolyzing β-lactamase SFC-1 from Serratia fonticola UTAD54 was overexpressed in Escherichia coli, purified, and characterized. The enzyme exhibited an apparent molecular mass of 30.5 kDa, determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. SFC-1 hydrolyzes penicillins, cephalosporins, aztreonam, and carbapenems and is inhibited by clavulanic acid, sulbactam, and tazobactam.",

author = "F{\'a}tima Fonseca and Sarmento, \{Ana Cristina\} and Isabel Henriques and Bart Samyn and \{Van Beeumen\}, Jozef and Pedro Domingues and Domingues, \{Maria Ros{\'a}rio\} and Saavedra, \{Maria Jos{\'e}\} and Ant{\'o}nio Correia",

year = "2007",

month = dec,

doi = "10.1128/AAC.00491-07",

language = "English",

volume = "51",

pages = "4512--4514",

journal = "Antimicrobial Agents and Chemotherapy",

issn = "0066-4804",

publisher = "American Society for Microbiology",

number = "12",

}

TY - JOUR

T1 - Biochemical characterization of SFC-1, a class A carbapenem-hydrolyzing β-lactamase

AU - Fonseca, Fátima

AU - Sarmento, Ana Cristina

AU - Henriques, Isabel

AU - Samyn, Bart

AU - Van Beeumen, Jozef

AU - Domingues, Pedro

AU - Domingues, Maria Rosário

AU - Saavedra, Maria José

AU - Correia, António

PY - 2007/12

Y1 - 2007/12

N2 - The carbapenem-hydrolyzing β-lactamase SFC-1 from Serratia fonticola UTAD54 was overexpressed in Escherichia coli, purified, and characterized. The enzyme exhibited an apparent molecular mass of 30.5 kDa, determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. SFC-1 hydrolyzes penicillins, cephalosporins, aztreonam, and carbapenems and is inhibited by clavulanic acid, sulbactam, and tazobactam.

AB - The carbapenem-hydrolyzing β-lactamase SFC-1 from Serratia fonticola UTAD54 was overexpressed in Escherichia coli, purified, and characterized. The enzyme exhibited an apparent molecular mass of 30.5 kDa, determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. SFC-1 hydrolyzes penicillins, cephalosporins, aztreonam, and carbapenems and is inhibited by clavulanic acid, sulbactam, and tazobactam.

UR - https://www.scopus.com/pages/publications/36749039667

U2 - 10.1128/AAC.00491-07

DO - 10.1128/AAC.00491-07

M3 - Article

C2 - 17875998

AN - SCOPUS:36749039667

SN - 0066-4804

VL - 51

SP - 4512

EP - 4514

JO - Antimicrobial Agents and Chemotherapy

JF - Antimicrobial Agents and Chemotherapy

IS - 12

ER -

Biochemical characterization of SFC-1, a class A carbapenem-hydrolyzing β-lactamase

Abstract

Access to Document

Other files and links

Fingerprint

Cite this