Luiz Pedro Sorio de Carvalho

Luiz Pedro Sorio de Carvalho, Ph.D.


Business Phone: (561) 228-2209
Business Email:

About Luiz Pedro Sorio de Carvalho

Additional Positions:
Visiting Group Leader
2023 – 2024 · The Francis Crick Institute
Principal Group Leader
2017 – 2023 · The Francis Crick Institute
Group Leader (tenure track)
2015 – 2017 · The Francis Crick Institute
Junior Group Leader (tenure track)
2011 – 2015 · MRC National Institute for Medical Research
Postdoctoral Fellow
2006 – 2011 · Weill Cornell Medical College


ACS Infectious Diseases/Biological Chemistry Division Young Investigator Award
2021 · American Chemical Society
Horizon Award (Group effort, included two lab members)
2021 · Royal Society of Chemistry
Irving S. Sigal Memorial Award
2014 · American Society for Microbiology
New Investigator Award
2014 · Wellcome Trust
MRC Centenary Early Career Award
2012 · Medical Research Council (MRC)

Research Profile

Diseases caused by bacteria from the genus Mycobacterium afflict humankind for millennia and currently represent a significant source of mortality and morbidity. Examples are human tuberculosis, leprosy, Buruli ulcer and other soft-tissue and lung infections. Tuberculosis alone is still responsible for 1.5 million deaths annually. The increased prevalence of antibiotic resistance in mycobacteria is a significant problem, causing nearly untreatable infections. The Carvalho group is interested in defining how soil-dwelling and water-born mycobacteria became adapted to the human host, a pre-requisite for a human pathogen. In particular, our group is focused on understanding how mycobacterial metabolism and chemistry evolved in the last 50 million years, to allow for optimal growth and virulence in humans. Once these processes have been mapped and characterized at cellular and molecular levels, we will employ state-of-the-art methods, some of which have been pioneered at UF Scripps, to discover and develop novel small molecules capable of killing these pathogens and transform the therapy of tuberculosis and other mycobacterial diseases.

Key recent advances include:

(i) discovery of the first example of target-mediated antibiotic inactivation

(ii) identification of the metabolic requirements for pyruvate and lactate utilization by M. tuberculosis

(iii) discovery of itaconate catabolism in M. tuberculosis and its intersection with amino acid metabolism

(iv) carried out the first fine mapping of nitrogen metabolism in M. tuberculosis.

(v) demonstration of the crucial role of metabolism in bacterial L-form

(vi) discovery of the first NAD+ phosphorylase and its role in M. tuberculosis cell death

Open Researcher and Contributor ID (ORCID)



A new strategy for hit generation: Novel in cellulo active inhibitors of CYP121A1 from Mycobacterium tuberculosis via a combined X-ray crystallographic and phenotypic screening approach (XP screen)
European Journal of Medicinal Chemistry. 230 [DOI] 10.1016/j.ejmech.2022.114105. [PMID] 35065413.
Gene–drug potency screening in M. tuberculosis
Nature Microbiology. 7(6):743-744 [DOI] 10.1038/s41564-022-01139-3.
Functional Characterization of the γ-Aminobutyric Acid Transporter from Mycobacterium smegmatis MC 2 155 Reveals Sodium-Driven GABA Transport
Journal of Bacteriology. 203(4) [DOI] 10.1128/jb.00642-20.
Human Mat2A Uses an Ordered Kinetic Mechanism and Is Stabilized but Not Regulated by Mat2B
Biochemistry. 60(47):3621-3632 [DOI] 10.1021/acs.biochem.1c00672. [PMID] 34780697.
d-Cycloserine destruction by alanine racemase and the limit of irreversible inhibition
Nature Chemical Biology. 16(6):686-694 [DOI] 10.1038/s41589-020-0498-9. [PMID] 32203411.
Mycobacterium tuberculosisrequires glyoxylate shunt and reverse methylcitrate cycle for lactate and pyruvate metabolism
Molecular Microbiology. 112(4):1284-1307 [DOI] 10.1111/mmi.14362. [PMID] 31389636.
An essential bifunctional enzyme in Mycobacterium tuberculosis for itaconate dissimilation and leucine catabolism
Proceedings of the National Academy of Sciences. 116(32):15907-15913 [DOI] 10.1073/pnas.1906606116. [PMID] 31320588.
An NAD+ Phosphorylase Toxin Triggers Mycobacterium tuberculosis Cell Death
Molecular Cell. 73(6):1282-1291.e8 [DOI] 10.1016/j.molcel.2019.01.028. [PMID] 30792174.
Author response: Flexible nitrogen utilisation by the metabolic generalist pathogen Mycobacterium tuberculosis
. [DOI] 10.7554/elife.41129.020.
Comparative fitness analysis of D-cycloserine resistant mutants reveals both fitness-neutral and high-fitness cost genotypes
Nature Communications. 10(1) [DOI] 10.1038/s41467-019-12074-z. [PMID] 31519879.
Crucial role for central carbon metabolism in the bacterial L-form switch and killing by β-lactam antibiotics
Nature Microbiology. 4(10):1716-1726 [DOI] 10.1038/s41564-019-0497-3. [PMID] 31285586.
Flexible nitrogen utilisation by the metabolic generalist pathogen Mycobacterium tuberculosis
eLife. 8 [DOI] 10.7554/elife.41129.
Streptococcal dTDP‐L‐rhamnose biosynthesis enzymes: functional characterization and lead compound identification
Molecular Microbiology. 111(4):951-964 [DOI] 10.1111/mmi.14197. [PMID] 30600561.
Synthesis and biological evaluation of novel cYY analogues targeting Mycobacterium tuberculosis CYP121A1
Bioorganic & Medicinal Chemistry. 27(8):1546-1561 [DOI] 10.1016/j.bmc.2019.02.051. [PMID] 30837169.
The tuberculosis necrotizing toxin is an NAD+ and NADP+ glycohydrolase with distinct enzymatic properties
Journal of Biological Chemistry. 294(9):3024-3036 [DOI] 10.1074/jbc.ra118.005832.
“Salmonella, meet mycobacteria.”
Journal of Experimental Medicine. 216(4):721-722 [DOI] 10.1084/jem.20190065. [PMID] 30824477.
The Mechanism of Acetyl Transfer Catalyzed by Mycobacterium tuberculosis GlmU
Biochemistry. 57(24):3387-3401 [DOI] 10.1021/acs.biochem.8b00121. [PMID] 29684272.
Inhibition of D-Ala:D-Ala ligase through a phosphorylated form of the antibiotic D-cycloserine
Nature Communications. 8(1) [DOI] 10.1038/s41467-017-02118-7. [PMID] 29208891.
Uncoupling conformational states from activity in an allosteric enzyme
Nature Communications. 8(1) [DOI] 10.1038/s41467-017-00224-0. [PMID] 28781362.
Glutamate Racemase Is the Primary Target of β-Chloro- d -Alanine in Mycobacterium tuberculosis
Antimicrobial Agents and Chemotherapy. 60(10):6091-6099 [DOI] 10.1128/aac.01249-16.
. [DOI] 10.35802/104785.
Antibiotic resistance evasion is explained by rare mutation frequency and not by lack of compensatory mechanisms
. [DOI] 10.1101/374215.
Discovery of a novel stereospecific β-hydroxyacyl-CoA lyase/thioesterase shared by three metabolic pathways inMycobacterium tuberculosis
. [DOI] 10.1101/322404.
Nitrogen utilisation by the metabolic generalist pathogen Mycobacterium tuberculosis
. [DOI] 10.1101/385278.


Ph.D. in Biochemistry
2006 · Albert Einstein College of Medicine
M.Sc. in Cell and Molecular Biology
2001 · Federal University of Rio Grande do Sul
Pharmacy Degree
1999 · Federal University of Rio Grande do Sul

Contact Details

(561) 228-2209
Business Street: