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microcin E492 biosynthetic process by siderophore ester modification of peptidyl-serine

Known as: microcin E492 anabolism by siderophore ester modification of peptidyl-serine, microcin E492 formation by siderophore ester modification of peptidyl-serine, microcin E492 synthesis by siderophore ester modification of peptidyl-serine 
The modification of serine to N-[5-(6-O-seryl-beta-glucosyl)-2,3-dihydroxybenzoyl]-O-[N-(2,3-dihydroxybenzoyl)-O-[N-(2,3-dihydroxybenzoyl)seryl]seryl… 
National Institutes of Health

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Highly Cited
2015
Highly Cited
2015
Lasso peptides are bacterial ribosomally synthesized and post-translationally modified peptides. They have sparked increasing… 
Highly Cited
2012
Highly Cited
2012
Microcin J25 is a potent antibacterial peptide produced by Escherichia coli AY25. It displays a lasso structure, which consists… 
Review
2009
Review
2009
Microcins are a family of low-molecular weight bacteriocins produced and secreted by Gram-negative bacteria. This review is… 
Highly Cited
2007
Highly Cited
2007
The present work reveals that four proteins, MceCDIJ, encoded by the MccE492 gene cluster are responsible for the remarkable post… 
Highly Cited
2002
Highly Cited
2002
A mutation in the conserved segment of therpoC gene, which codes for the largest RNA polymerase (RNAP) subunit, β′, was found to… 
Highly Cited
2002
Highly Cited
2002
The cytotoxic effect of microcin E492, a low-molecular-mass channel-forming bacteriocin (7,887 Da) produced by a strain of… 
Highly Cited
2001
Highly Cited
2001
Microcin E492 is a low‐molecular‐weight, channel‐forming bacteriocin produced and excreted by Klebsiella pneumoniae RYC492. A 13… 
Highly Cited
2000
Highly Cited
2000
ABSTRACT The inhibitory activities of known microcins were evaluated against some diarrheagenic Escherichia coli strains. Some… 
Highly Cited
1985
Highly Cited
1985
Microcin E492 is a 5,000- to 7,000-molecular-weight peptide antibiotic which depolarizes the cytoplasmic membrane of sensitive…