ArticleThe Journal of biological chemistry2010
Active site metal ion in UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) switches between Fe(II) and Zn(II) depending on cellular conditions.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 42 citations in OpenAlex.
- The HypA and HypB metallochaperones from Methanococcus maripaludis have unique metal-binding properties and a distinct nickel transfer mechanism.The Journal of biological chemistry · 2026Article
- Biology of novel LpxC inhibitors forMicrobiology spectrum · 2026Article
- The activation of the metal-containing regulatory protein NiaR from Thermotoga maritima by its effector, nicotinic acid.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025Article
- Properties and biotechnological applications of microbial deacetylase.Applied microbiology and biotechnology · 2023Review
- How Theoretical Evaluations Can Generate Guidelines for Designing/Engineering Metalloproteins with Desired Metal Affinity and Selectivity.Molecules (Basel, Switzerland) · 2022Review
- Metal cofactor stabilization by a partner protein is a widespread strategy employed for amidase activation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structure- and Ligand-Dynamics-Based Design of Novel Antibiotics Targeting Lipid A Enzymes LpxC and LpxH in Gram-Negative Bacteria.Accounts of chemical research · 2021Review
- An Acinetobacter baumannii, Zinc-Regulated Peptidase Maintains Cell Wall Integrity during Immune-Mediated Nutrient Sequestration.Cell reports · 2019Article
- Fast Screening of Inhibitor Binding/Unbinding Using Novel Software Tool CaverDock.Frontiers in chemistry · 2019Article
- Structure, inhibition, and regulation of essential lipid A enzymes.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017Review
- Active Site Metal Identity Alters Histone Deacetylase 8 Substrate Selectivity: A Potential Novel Regulatory Mechanism.Biochemistry · 2017Article
- The Metal Drives the Chemistry: Dual Functions of Acireductone Dioxygenase.Chemical reviews · 2017Review
- Kinetics and thermodynamics of metal-binding to histone deacetylase 8.Protein science : a publication of the Protein Society · 2015Article
- The DNA uptake ATPase PilF of Thermus thermophilus: a reexamination of the zinc content.Extremophiles : life under extreme conditions · 2013Article
- The structure- and metal-dependent activity of Escherichia coli PgaB provides insight into the partial de-N-acetylation of poly-β-1,6-N-acetyl-D-glucosamine.The Journal of biological chemistry · 2012Article
- ZntR-mediated transcription of zntA responds to nanomolar intracellular free zinc.Journal of inorganic biochemistry · 2012Article
- Elemental economy: microbial strategies for optimizing growth in the face of nutrient limitation.Advances in microbial physiology · 2012Review
- Genetically encoded ratiometric biosensors to measure intracellular exchangeable zinc in Escherichia coli.Journal of biomedical optics · 2011Article
- The activity and cofactor preferences of N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase (MshB) change depending on environmental conditions.The Journal of biological chemistry · 2011Article
- Control of lipopolysaccharide biosynthesis by FtsH-mediated proteolysis of LpxC is conserved in enterobacteria but not in all gram-negative bacteria.Journal of bacteriology · 2011Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) catalyzes the deacetylation of UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate in Gram-negative bacteria. This second, and committed, step in lipid A biosynthesis is a target for antibiotic development. LpxC was previously identified as a mononuclear Zn(II) metalloenzyme; however, LpxC is 6-8-fold more active with the oxygen-sensitive Fe(II) cofactor (Hernick, M., Gattis, S. G., Penner-Hahn, J. E., and Fierke, C. A. (2010) Biochemistry 49, 2246-2255). To analyze the native metal cofactor bound to LpxC, we developed a pulldown method to rapidly purify tagged LpxC under anaerobic conditions. The metal bound to LpxC purified from Escherichia coli grown in minimal medium is mainly Fe(II). However, the ratio of iron/zinc bound to LpxC varies with the metal content of the medium. Furthermore, the iron/zinc ratio bound to native LpxC, determined by activity assays, has a similar dependence on the growth conditions. LpxC has significantly higher affinity for Zn(II) compared with Fe(II) with K(D) values of 60 ± 20 pM and 110 ± 40 nM, respectively. However, in vivo concentrations of readily exchangeable iron are significantly higher than zinc, suggesting that Fe(II) is the thermodynamically favored metal cofactor for LpxC under cellular conditions. These data indicate that LpxC expressed in E. coli grown in standard medium predominantly exists as the Fe(II)-enzyme. However, the metal cofactor in LpxC can switch between iron and zinc in response to perturbations in available metal ions. This alteration may be important for regulating the LpxC activity upon changes in environmental conditions and may be a general mechanism of regulating the activity of metalloenzymes.
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