Unusual metallo-beta-lactamases may constitute a new subgroup in this family of enzymes

Hou, Chun-Feng D., Phelan, Emer K., Miraula, Manfredi, Ollis, David L., Schenk, Gerhard and Mitić, Nataša (2014) Unusual metallo-beta-lactamases may constitute a new subgroup in this family of enzymes. American Journal of Molecular Biology, 4 1: 11-15. doi:10.4236/ajmb.2014.41002


Author Hou, Chun-Feng D.
Phelan, Emer K.
Miraula, Manfredi
Ollis, David L.
Schenk, Gerhard
Mitić, Nataša
Title Unusual metallo-beta-lactamases may constitute a new subgroup in this family of enzymes
Formatted title
Unusual metallo-β-lactamases may constitute a new subgroup in this family of enzymes
Journal name American Journal of Molecular Biology   Check publisher's open access policy
ISSN 2161-6620
2161-6663
Publication date 2014-01-15
Sub-type Article (original research)
DOI 10.4236/ajmb.2014.41002
Open Access Status DOI
Volume 4
Issue 1
Start page 11
End page 15
Total pages 5
Place of publication Irvine, CA, United States
Publisher Scientific Research Publishing
Collection year 2015
Language eng
Formatted abstract
Metallo-β-lactamases (MBLs) are a family of Zn2+-dependent enzymes that have contributed strongly to the emergence and spread of antibiotic resistance. Novel members as well as variants of existing members of this family are discovered continuously, compounding their threat to global health care. MBLs are divided into three subgroups, i.e. B1, B2 and B3. The recent discovery of an unusual MBL from Serratia proteamaculans (SPR-1) suggests the presence of an additional subgroup, i.e. B4. A database search reveals that SPR-1 has only one homologue from Cronobacter sakazakii, CSA-1.These two MBLs have a unique active site and may employ a mechanism distinct from other MBLs, but reminiscent of some organophosphate-degrading hydrolases.
Keyword Antibiotic resistance
β-Lactam antibiotics
Metallo-β-lactamases
Sequence homology
Serratia proteamaculans
Cronobacter sakazakii
beta-Lactam antibiotics
Metallo-beta-lactamases
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2015 Collection
School of Chemistry and Molecular Biosciences
 
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Created: Thu, 07 Aug 2014, 13:25:26 EST by Associate Professor Gary Schenk on behalf of School of Chemistry & Molecular Biosciences