Cited by 185Microbial metabolism and enzyme functionMicrobial Metabolic Engineering and BioproductionBacterial Genetics and Biotechnology

The DOI matches its Crossref record; 85 of the 85 references it cites were found in a registry or an index.

The Glyoxylate Shunt, 60 Years On

Dolan, Stephen K., Welch, Martin·2018·Annual Review of Microbiology

DOI 10.1146/annurev-micro-090817-062257

Open this paper in CoChat — free account

Abstract

2017 marks the 60th anniversary of Krebs’ seminal paper on the glyoxylate shunt (and coincidentally, also the 80th anniversary of his discovery of the citric acid cycle). Sixty years on, we have witnessed substantial developments in our understanding of how flux is partitioned between the glyoxylate shunt and the oxidative decarboxylation steps of the citric acid cycle. The last decade has shown us that the beautifully elegant textbook mechanism that regulates carbon flux through the shunt in E. coli is an oversimplification of the situation in many other bacteria. The aim of this review is to assess how this new knowledge is impacting our understanding of flux control at the TCA cycle/glyoxylate shunt branch point in a wider range of genera, and to summarize recent findings implicating a role for the glyoxylate shunt in cellular functions other than metabolism.

Integrity signals

Registry

Crossref · 10.1146/annurev-micro-090817-062257

Cites

85 of 85 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Requirement of NAD and SIR2 for Life-Span Extension by Calorie Restriction in Saccharomyces cerevisiae
Lin, S.-J., Defossez, P.-A., & Guarente, L. (2000) · Science · doi:10.1126/science.289.5487.2126 · Cited by 1,775
Persistence of Mycobacterium tuberculosis in macrophages and mice requires the glyoxylate shunt enzyme isocitrate lyase
McKinney, J. D., zu Bentrup, K. H., Muñoz‐Elías, E. J., Miczák, A., Chen, B., Chan, W.-T., Swenson, D. L., Sacchettini, J. C., Jacobs, W. R., & Russell, D. G. (2000) · Nature · doi:10.1038/35021074 · Cited by 1,361
Acetylation of Metabolic Enzymes Coordinates Carbon Source Utilization and Metabolic Flux
Wang, Q., Zhang, Y., Yang, C., Xiong, H., Lin, Y., Yao, J., Li, H., Xie, L., Zhao, W., Yao, Y., et al. (2010) · Science · doi:10.1126/science.1179687 · Cited by 1,008
The type III secretion system of Pseudomonas aeruginosa: infection by injection
Hauser, A. R. (2009) · Nature Reviews Microbiology · doi:10.1038/nrmicro2199 · Cited by 971
Mycobacterium tuberculosis isocitrate lyases 1 and 2 are jointly required for in vivo growth and virulence
Muñoz‐Elías, E. J., & McKinney, J. D. (2005) · Nature Medicine · doi:10.1038/nm1252 · Cited by 760
Synthesis of Cell Constituents from C2-Units by a Modified Tricarboxylic Acid Cycle
Kornberg, H. L., & Krebs, H. A. (1957) · Nature · doi:10.1038/179988a0 · Cited by 611
The role and control of the glyoxylate cycle in Escherichia coli
Kornberg, H. L. (1966) · Biochemical Journal · doi:10.1042/bj0990001 · Cited by 608
Lysine Acetylation Is a Highly Abundant and Evolutionarily Conserved Modification in Escherichia Coli
Zhang, J., Sprung, R. W., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C., Grishin, N. V., & Zhao, Y. (2008) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800187-mcp200 · Cited by 474
Carbon Sources Tune Antibiotic Susceptibility in Pseudomonas aeruginosa via Tricarboxylic Acid Cycle Control
Meylan, S., Porter, C. B. M., Yang, J. H., Belenky, P. A., Gutierrez, A., Lobritz, M. A., Park, J., Kim, S. H., Moskowitz, S. M., & Collins, J. J. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2016.12.015 · Cited by 384
3-Nitropropionate, the toxic substance of Indigofera , is a suicide inactivator of succinate dehydrogenase
Alston, T. A., Mela, L., & Bright, H. J. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.9.3767 · Cited by 382
Role of the methylcitrate cycle in Mycobacterium tuberculosis metabolism, intracellular growth, and virulence
Muñoz‐Elías, E. J., Upton, A. M., Cherian, J., & McKinney, J. D. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05155.x · Cited by 370
The Tricarboxylic Acid Cycle in Cyanobacteria
Zhang, S., & Bryant, D. A. (2011) · Science · doi:10.1126/science.1210858 · Cited by 368
Requirements for Pseudomonas aeruginosa Acute Burn and Chronic Surgical Wound Infection
Turner, K. H., Everett, J. A., Trivedi, U., Rumbaugh, K. P., & Whiteley, M. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004518 · Cited by 352
Isocitrate lyase mediates broad antibiotic tolerance in Mycobacterium tuberculosis
Nandakumar, M., Nathan, C., & Rhee, K. Y. (2014) · Nature Communications · doi:10.1038/ncomms5306 · Cited by 298
Role of Glyoxylate Shunt in Oxidative Stress Response
Ahn, S., Jung, J., Jang, I.-A., Madsen, E. L., & Park, W. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.708149 · Cited by 280
Characterization of Activity and Expression of Isocitrate Lyase in Mycobacterium avium and Mycobacterium tuberculosis
zu Bentrup, K. H., Miczák, A., Swenson, D. L., & Russell, D. G. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.23.7161-7167.1999 · Cited by 278
Identification of the Protein Acetyltransferase (Pat) Enzyme that Acetylates Acetyl-CoA Synthetase in Salmonella enterica
Starai, V. J., & Escalante‐Semerena, J. C. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.05.010 · Cited by 260
Structure of isocitrate lyase, a persistence factor of Mycobacterium tuberculosis.
Sharma, V., Sharma, S., zu Bentrup, K. H., McKinney, J. D., Russell, D. G., Jacobs, W. R., & Sacchettini, J. C. (2000) · Nature Structural Biology · doi:10.1038/77964 · Cited by 254
The role of citric acid in intermediate metabolism in animal tissues
Krebs, H. A., & Johnson, W. A. (1980) · FEBS Letters · doi:10.1016/0014-5793(80)80564-3 · Cited by 249
Phosphorylation of Isocitrate Dehydrogenase of Escherichia coli
Garnak, M., & Reeves, H. C. (1979) · Science · doi:10.1126/science.34215 · Cited by 241
Bacterial itaconate degradation promotes pathogenicity
Sasikaran, J., Ziemski, M., Zadora, P. K., Fleig, A., & Berg, I. A. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1482 · Cited by 224
Itaconate, an isocitrate lyase-directed inhibitor in Pseudomonas indigofera
McFadden, B. A., & Purohit, S. (1977) · Journal of Bacteriology · doi:10.1128/jb.131.1.136-144.1977 · Cited by 220
A protein with kinase and phosphatase activities involved in regulation of tricarboxylic acid cycle
LaPorte, D. C., & Koshland, D. E. (1982) · Nature · doi:10.1038/300458a0 · Cited by 215
Phosphorylation of isocitrate dehydrogenase as a demonstration of enhanced sensitivity in covalent regulation
LaPorte, D. C., & Koshland, D. E. (1983) · Nature · doi:10.1038/305286a0 · Cited by 190
Dual role of isocitrate lyase 1 in the glyoxylate and methylcitrate cycles in Mycobacterium tuberculosis
Gould, T. A., van de Langemheen, H., Muñoz‐Elías, E. J., McKinney, J. D., & Sacchettini, J. C. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05297.x · Cited by 187
The branch point effect. Ultrasensitivity and subsensitivity to metabolic control.
LaPorte, D. C., Walsh, K., & Koshland, D. E. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)89857-x · Cited by 180
REGULATION OF ACETATE METABOLISM BY PROTEIN PHOSPHORYLATION IN ENTERIC BACTERIA
Cozzone, A. J. (1998) · Annual Review of Microbiology · doi:10.1146/annurev.micro.52.1.127 · Cited by 180
Determination of flux through the branch point of two metabolic cycles. The tricarboxylic acid cycle and the glyoxylate shunt.
Walsh, K., & Koshland, D. E. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42750-5 · Cited by 175
Methylcitrate cycle defines the bactericidal essentiality of isocitrate lyase for survival of Mycobacterium tuberculosis on fatty acids
Eoh, H., & Rhee, K. Y. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1400390111 · Cited by 171
Citric‐acid cycle, 50 years on
Thauer, R. K. (1988) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1988.tb14307.x · Cited by 166
Protein-protein interactions and metabolite channelling in the plant tricarboxylic acid cycle
Zhang, Y., Beard, K. F. M., Swart, C., Bergmann, S., Krahnert, I., Nikoloski, Z., Graf, A., Ratcliffe, R. G., Sweetlove, L. J., Fernie, A. R., et al. (2017) · Nature Communications · doi:10.1038/ncomms15212 · Cited by 159
Role of the methylcitrate cycle in propionate metabolism and detoxification in Mycobacterium smegmatis
Upton, A. M., & McKinney, J. D. (2007) · Microbiology · doi:10.1099/mic.0.2007/011726-0 · Cited by 151
Biochemical and Structural Studies of Malate Synthase fromMycobacterium tuberculosis
Smith, C. V., Huang, C.-C., Miczák, A., Russell, D. G., Sacchettini, J. C., & zu Bentrup, K. H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209248200 · Cited by 150
Synthesis of C4-dicarboxylic acids from acetate by a “glyoxylate bypass” of the tricarboxylic acid cycle
Kornberg, H. L., & Madsen, N. B. (1957) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(57)90268-8 · Cited by 150
Metabolic Engineering of TCA Cycle for Production of Chemicals
Vuoristo, K. S., Mars, A. E., Sanders, J. P. M., Eggink, G., & Weusthuis, R. A. (2015) · Trends in biotechnology · doi:10.1016/j.tibtech.2015.11.002 · Cited by 145
The Selective Cause of an Ancient Adaptation
Zhu, G., Golding, G. B., & Dean, A. M. (2005) · Science · doi:10.1126/science.1106974 · Cited by 141
Compensatory phosphorylation of isocitrate dehydrogenase. A mechanism for adaptation to the intracellular environment.
LaPorte, D. C., Thorsness, P. E., & Koshland, D. E. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85122-0 · Cited by 138
RamB, a Novel Transcriptional Regulator of Genes Involved in Acetate Metabolism of Corynebacterium glutamicum
Gerstmeir, R., Cramer, A., Dangel, P., Schaffer, S., & Eikmanns, B. J. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.9.2798-2809.2004 · Cited by 132
CONVERSION OF ACETATE AND GLYOXYLATE TO MALATE1
Ajl, S. J. (1956) · Journal of the American Chemical Society · doi:10.1021/ja01594a079 · Cited by 126
Structure-Guided Discovery of Phenyl-diketo Acids as Potent Inhibitors of M. tuberculosis Malate Synthase
Krieger, I. V., Freundlich, J. S., Gawandi, V., Roberts, J. P., Gawandi, V. B., Sun, Q., Owen, J. L., Fraile, M., Huss, S. I., Lavandera, J.-L., et al. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.09.018 · Cited by 125
Direct Evidence for Metabolon Formation and Substrate Channeling in Recombinant TCA Cycle Enzymes
Bulutoglu, B., Garcia, K. E., Wu, F., Minteer, S. D., & Banta, S. A. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00523 · Cited by 116
Regulation of Glucose Metabolism in Pseudomonas
Daddaoua, A., Krell, T., & Ramos, J. L. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.014555 · Cited by 111
Isocitrate Lyase (AceA) Is Required for Salmonella Persistence but Not for Acute Lethal Infection in Mice
Fang, F. C., Libby, S. J., Castor, M. E., & Fung, A. M. (2005) · Infection and Immunity · doi:10.1128/iai.73.4.2547-2549.2005 · Cited by 107
The metabolism of C2 compounds in micro-organisms. 1. The incorporation of [2-14C]acetate by Pseudomonas fluorescens, and by a Corynebacterium, grown on ammonium acetate
Kornberg, H. L. (1958) · Biochemical Journal · doi:10.1042/bj0680535 · Cited by 104
Regulated expression of a repressor protein: FadR activates iclR
Gui, L., Sunnarborg, A., & LaPorte, D. C. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.15.4704-4709.1996 · Cited by 104
Novel Metabolic Attributes of the Genus Cyanothece , Comprising a Group of Unicellular Nitrogen-Fixing Cyanobacteria
Bandyopadhyay, A., Elvitigala, T., Welsh, E., Stöckel, J., Liberton, M., Min, H., Sherman, L. A., & Pakrasi, H. B. (2011) · mBio · doi:10.1128/mbio.00214-11 · Cited by 102
Glyoxylate detoxification is an essential function of malate synthase required for carbon assimilation in Mycobacterium tuberculosis
Puckett, S. E., Trujillo, C., Wang, Z., Eoh, H., Ioerger, T. R., Krieger, I. V., Sacchettini, J. C., Schnappinger, D., Rhee, K. Y., & Ehrt, S. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1617655114 · Cited by 100
Protein engineering reveals ancient adaptive replacements in isocitrate dehydrogenase
Dean, A. M., & Golding, G. B. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.7.3104 · Cited by 94
Glyoxylate bypass operon of Escherichia coli: cloning and determination of the functional map
Chung, T., Klumpp, D. J., & LaPorte, D. C. (1988) · Journal of Bacteriology · doi:10.1128/jb.170.1.386-392.1988 · Cited by 89
Virulence determinants from a cystic fibrosis isolate of Pseudomonas aeruginosa include isocitrate lyase
Lindsey, T. L., Hagins, J. M., Sokol, P. A., & Silo-Suh, L. (2008) · Microbiology · doi:10.1099/mic.0.2007/014506-0 · Cited by 88
The isocitrate dehydrogenase phosphorylation cycle: Regulation and enzymology
LaPorte, D. C. (1993) · Journal of Cellular Biochemistry · doi:10.1002/jcb.240510104 · Cited by 87
Glyoxylate and Pyruvate Are Antagonistic Effectors of the Escherichia coli IclR Transcriptional Regulator
Lorca, G. L., Ezersky, A., Lunin, V. V., Walker, J. R., Altamentova, S., Evdokimova, E., Vedadi, M., Bochkarev, A., & Savchenko, A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610838200 · Cited by 87
Krebs and his trinity of cycles
Kornberg, H. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35043073 · Cited by 86
Biochemical Validation of the Glyoxylate Cycle in the Cyanobacterium Chlorogloeopsis fritschii Strain PCC 9212
Zhang, S., & Bryant, D. A. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.648170 · Cited by 86
ISOCITRITASE: A NEW TRICARBOXYLIC ACID CLEAVAGE SYSTEM
Smith, R. A., & GUNSALUS, I. C. (1954) · Journal of the American Chemical Society · doi:10.1021/ja01648a084 · Cited by 84
Regulation of the acetate operon in Escherichia coli: purification and functional characterization of the IclR repressor.
Cortay, J., Négre, D., Galinier, A., Duclos, B., Perrière, G., & Cozzone, A. J. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07996.x · Cited by 82
System-wide Studies of N-Lysine Acetylation in Rhodopseudomonas palustris Reveal Substrate Specificity of Protein Acetyltransferases
Crosby, H. A., Pelletier, D. A., Hurst, G. B., & Escalante‐Semerena, J. C. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.352104 · Cited by 82
The regulatory properties of isocitrate dehydrogenase kinase and isocitrate dehydrogenase phosphatase from Escherichia coli ML308 and the roles of these activities in the control of isocitrate dehydrogenase
Nimmo, G. A., & Nimmo, H. G. (1984) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1984.tb08206.x · Cited by 78
Structure of the bifunctional isocitrate dehydrogenase kinase/phosphatase
Zheng, J., & Jia, Z. (2010) · Nature · doi:10.1038/nature09088 · Cited by 74
A reverse glyoxylate shunt to build a non-native route from C4 to C2 in Escherichia coli
Mainguet, S. E., Gronenberg, L. S., Wong, S. S., & Liao, J. C. (2013) · Metabolic Engineering · doi:10.1016/j.ymben.2013.06.004 · Cited by 72
Genes encoding two isocitrate dehydrogenase isozymes of a psychrophilic bacterium, Vibrio sp. strain ABE-1
Ishii, A., Suzuki, M., Sahara, T., Takada, Y., Sasaki, S., & Fukunaga, N. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.21.6873-6880.1993 · Cited by 66
Kinetic modeling of tricarboxylic acid cycle and glyoxylate bypass in Mycobacterium tuberculosis, and its application to assessment of drug targets
Singh, V. K., & Ghosh, I. (2006) · Theoretical Biology and Medical Modelling · doi:10.1186/1742-4682-3-27 · Cited by 64
Reversible acetylation regulates acetate and propionate metabolism in Mycobacterium smegmatis
Hayden, J., Brown, L. R., Gunawardena, H. P., Perkowski, E. F., Chen, X., & Braunstein, M. (2013) · Microbiology · doi:10.1099/mic.0.068585-0 · Cited by 57
A Novel Role of the PrpR as a Transcription Factor Involved in the Regulation of Methylcitrate Pathway in Mycobacterium tuberculosis
Masiewicz, P., Brzostek, A. M., Wolański, M., Dziadek, J., & Zakrzewska‐Czerwińska, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0043651 · Cited by 55
Non-Traditional Antibacterial Screening Approaches for the Identification of Novel Inhibitors of the Glyoxylate Shunt in Gram-Negative Pathogens
Fahnoe, K. C., Flanagan, M. E., Gibson, G., Shanmugasundaram, V., Che, Y., & Tomaras, A. P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0051732 · Cited by 53
Role of the Transcriptional Regulator RamB (Rv0465c) in the Control of the Glyoxylate Cycle in Mycobacterium tuberculosis
Micklinghoff, J. C., Breitinger, K. J., Schmidt, M., Geffers, R., Eikmanns, B. J., & Bange, F. (2009) · Journal of Bacteriology · doi:10.1128/jb.01009-09 · Cited by 53
Mechanism-based inactivator of isocitrate lyases 1 and 2 from Mycobacterium tuberculosis
Pham, T. V., Murkin, A. S., Moynihan, M. M., Harris, L. D., Tyler, P. C., Shetty, N. D., Sacchettini, J. C., Huang, H., & Meek, T. D. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1706134114 · Cited by 49
The structure and domain organization ofEscherichia coliisocitrate lyase
Britton, K. L., Abeysinghe, I. S. B., Baker, P. J., Barynin, V. V., Diehl, P., Langridge, S., McFadden, B. A., Sedelnikova, S. E., Stillman, T. J., Weeradechapon, K., et al. (2001) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444901008642 · Cited by 44
One ligand, two regulators and three binding sites: How KDPG controls primary carbon metabolism in Pseudomonas
Campilongo, R., Fung, R. K. Y., Little, R. H., Grenga, L., Trampari, E., Pepe, S., Chandra, G., Stevenson, C. E. M., Roncarati, D., & Malone, J. G. (2017) · PLoS Genetics · doi:10.1371/journal.pgen.1006839 · Cited by 42
Resistance to Diet-Induced Obesity in Mice with Synthetic Glyoxylate Shunt
Dean, J. T., Tran, L. M., Beaven, S. W., Tontonoz, P., Reue, K., Dipple, K. M., & Liao, J. C. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.04.008 · Cited by 41
Purification and regulatory properties of isocitrate lyase from Escherichia coli ML308
MacKintosh, C., & Nimmo, H. G. (1988) · Biochemical Journal · doi:10.1042/bj2500025 · Cited by 37
Bacillus subtilis Isocitrate Dehydrogenase
Singh, S. K., Miller, S. P., Dean, A. M., Banaszak, L. J., & LaPorte, D. C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107908200 · Cited by 33
Type III secretion system expression in oxygen-limited Pseudomonas aeruginosa cultures is stimulated by isocitrate lyase activity
Chung, J. C. S., Rzhepishevska, O. I., Ramstedt, M., & Welch, M. (2013) · Open Biology · doi:10.1098/rsob.120131 · Cited by 33
Self-citation
A rheostat mechanism governs the bifurcation of carbon flux in mycobacteria
Murima, P., Zimmermann, M., Chopra, T., Pojer, F., Fonti, G., Peraro, M. D., Alonso, S., Sauer, U., Pethe, K., & McKinney, J. D. (2016) · Nature Communications · doi:10.1038/ncomms12527 · Cited by 32
Locations of the Regulatory Sites for Isocitrate Dehydrogenase Kinase/Phosphatase
Miller, S. P., Chen, R., Karschnia, E. J., ROMFO, C. M., Dean, A. M., & LaPorte, D. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.2.833 · Cited by 24
Novel protein acetyltransferase, Rv2170, modulates carbon and energy metabolism in Mycobacterium tuberculosis
Lee, W., VanderVen, B. C., Walker, S., & Russell, D. G. (2017) · Scientific Reports · doi:10.1038/s41598-017-00067-1 · Cited by 23
Role of Phosphoenolpyruvate in the NADP-Isocitrate Dehydrogenase and Isocitrate Lyase Reaction in Escherichia coli
Ogawa, T., Murakami, K., Mori, H., Ishii, N., Tomita, M., & Yoshin, M. (2006) · Journal of Bacteriology · doi:10.1128/jb.01628-06 · Cited by 22
Complex formation between malate dehydrogenase and isocitrate dehydrogenase from Bacillus subtilis is regulated by tricarboxylic acid cycle metabolites
Bartholomae, M., Meyer, F. M., Commichau, F. M., Burkovski, A., Hillen, W., & Seidel, G. (2013) · FEBS Journal · doi:10.1111/febs.12679 · Cited by 22
The metabolism of C2 compounds in micro-organisms. 2. The effect of carbon dioxide on the incorporation of [14C]acetate by acetate-grown Pseudomonas KB1
Kornberg, H. L., & Quayle, J. R. (1958) · Biochemical Journal · doi:10.1042/bj0680542 · Cited by 22
A Specific Association Between the Glyoxylic‐Acid‐Cycle Enzymes Isocitrate Lyase and Malate Synthase
Beeckmans, S., Khan, A. S., DRIESSCHE, E. V., & Kanarek, L. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb20012.x · Cited by 20
Structural and Functional Characterization of Malate Synthase G from Opportunistic Pathogen Pseudomonas aeruginosa
McVey, A. C., Medarametla, P., Wezen, X. C., Bartlett, S., Poso, A., Spring, D. R., Rahman, T., & Welch, M. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00852 · Cited by 19
Self-citation
Evaluation of the Role of Constitutive Isocitrate Lyase Activity inYersinia pestisInfection of the Flea Vector and Mammalian Host
Sebbane, F., Jarrett, C. O., Linkenhoker, J., & Hinnebusch, B. J. (2004) · Infection and Immunity · doi:10.1128/iai.72.12.7334-7337.2004 · Cited by 17
Activity and functional properties of the isocitrate lyase in the cyanobacterium Cyanothece sp. PCC 7424
Gründel, M., Knoop, H., & Steuer, R. (2017) · Microbiology · doi:10.1099/mic.0.000459 · Cited by 14
Structural Basis of the Substrate Specificity of Bifunctional Isocitrate Dehydrogenase Kinase/Phosphatase
Yates, S. P., Edwards, T. E., Bryan, C. M., Stein, A. J., A, W. C. V. V., Myler, P. J., Stewart, L. J., Zheng, J., & Jia, Z. (2011) · Biochemistry · doi:10.1021/bi200809p · Cited by 13
Loopβ3αC plays an important role in the structure and function of isocitrate dehydrogenase kinase/phosphatase
Yin, Y., Li, S., Gao, Y., Tong, L., Zheng, J., Jia, Z., Jiang, G., & Wei, Q. (2016) · FEBS Letters · doi:10.1002/1873-3468.12355 · Cited by 2

Research works printed but not linked: 2

Bi J, 2017, Rep, 7, 44826
Castano-Cerezo S, 2014, Biol, 10, 762

Sorted by citations

Spatial transcriptomics of planktonic and sessile bacterial populations at single-cell resolution
Dar, D., Dar, N., Cai, L., & Newman, D. K. (2021) · Science · doi:10.1126/science.abi4882 · Cited by 303
Reactive oxygen species in pathogen clearance: The killing mechanisms, the adaption response, and the side effects
Li, H., Zhou, X., Huang, Y., Liao, B., Cheng, L., & Ren, B. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.622534 · Cited by 284
Phage-specific metabolic reprogramming of virocells
Howard‐Varona, C., Lindback, M., Bastien, G. E., Solonenko, N., Zayed, A. A., Jang, H. B., Andreopoulos, B., Brewer, H. M., del Rio, T. G., Adkins, J., et al. (2020) · The ISME Journal · doi:10.1038/s41396-019-0580-z · Cited by 239
Immunometabolic crosstalk during bacterial infection
Rosenberg, G., Riquelme, S. A., Prince, A. S., & Avraham, R. (2022) · Nature Microbiology · doi:10.1038/s41564-022-01080-5 · Cited by 152
Acetate as a potential feedstock for the production of value-added chemicals: Metabolism and applications
Kim, Y.-H., Lama, S., Agrawal, D., Kumar, V., & Park, S. (2021) · Biotechnology Advances · doi:10.1016/j.biotechadv.2021.107736 · Cited by 146

See all 185

Authors: Dolan, S. K., & Welch, M.
Affiliations: University of Cambridge (GB)
ORCID: Dolan, Stephen K.
Welch, Martin
Venue: Annual Review of Microbiology
Publisher: Annual Reviews
Published: 2018-09-08
Volume: 72
Issue: 1
Pages: 309-330
ISSN: 0066-4227 (ISSN-L)
1545-3251
DOI: 10.1146/annurev-micro-090817-062257
OpenAlex: W2892337114
Cited by: 180
References: 85
Citations by year: 2026: 33 · 2025: 24 · 2024: 19 · 2023: 22 · 2022: 20 · 2021: 25 · 2020: 27 · 2019: 9 · 2018: 1
FWCI: 1.52
Type: journal article
Language: en
Open access: closed
Locations: Annual Review of Microbiology (publishedVersion)
PubMed (publishedVersion)
Funders: Biotechnology and Biological Sciences Research Council (BB/R005435/1, BB/M019411/1)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial metabolism and enzyme function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial Metabolic Engineering and Bioproduction
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Keywords: glyoxylate cycle, TCA cycle, carbon flux partitioning, oxidative decarboxylation, flux control, Escherichia coli, bacterial metabolism
MeSH terms: Carbon, Escherichia coli, Glyoxylates, Metabolic Networks and Pathways, Metabolic Flux Analysis

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

The Glyoxylate Shunt, 60 Years On

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks