When attacked by macrophages\u2014immune cells that kill bacteria by engulfing them in an acidic intracellular compartment\u2014Mtb<\/em>\u00a0undergoes metabolic changes that allow it to subsist in severely nutrient-limited conditions (3<\/em><\/a>). The creative strategies that\u00a0Mtb<\/em>\u00a0uses to hide in this persistent state are still being discovered. For example, recent analysis of lipid profiles in patient-derived\u00a0Mtb<\/em>\u00a0strains revealed that the pathogen coats itself with a lipid- and nucleotide-derived antacid molecule (4<\/em><\/a>), which serves as chemical body armor for the macrophage-entrenched bacterium.<\/p>\n Mtb<\/em>-infected immune cells respond by diverting a common aerobic metabolite,\u00a0cis<\/em>-aconitate, to large-scale production of the host immunomodulator itaconate (5<\/em><\/a>). Although the antibacterial properties of itaconate have been known for more than 30 years, the recent discovery that it accumulates to millimolar concentrations in activated macrophages sparked renewed interest in its molecular mechanism. Itaconate can be appended to the key metabolic cofactor coenzyme A (CoA) to yield itaconyl-CoA (I-CoA). Itaconate and I-CoA resemble intermediates in bacterial pathways for lipid and amino acid catabolism, and their ability to inhibit metabolic enzymes in other bacteria suggested a possible route to itaconate-mediated growth inhibition in pathogens (5<\/em><\/a>). However, the precise target(s) of itaconate and modes of inhibition in\u00a0Mtb<\/em>\u00a0were unknown.<\/p>\n <\/p>\n MYCOBACTERIUM TUBERCULOSIS<\/em>\u00a0(MTB<\/em>) METHYLMALONYL\u2013COENZYME A (MM-COA) MUTASE USES A LONG TUNNEL TO BIND AND ORIENT ITS NATIVE SUBSTRATE MM-COA OR THE IRREVERSIBLE INACTIVATOR ITACONYL-COA (I-COA) NEAR A VITAMIN B12<\/sub>\u2013DERIVED COFACTOR. MM-COA AND I-COA EACH TRIGGER FORMATION OF A 5\u2032-DEOXYADENOSYL (5\u2032-DA\u2022) INTERMEDIATE.<\/p>\n <\/p>\n <\/p>\n Ruetz\u00a0et al.<\/em>\u00a0now address both questions by showing that I-CoA strongly inhibits\u00a0Mtb<\/em>\u00a0methylmalonyl-CoA mutase (MCM) by undergoing covalent attachment to the enzyme’s vitamin B12<\/sub>\u2013derived cobalamin (Cbl) cofactor. MCM promotes the carbon-skeleton rearrangement that converts its namesake substrate to succinyl-CoA. The reaction transforms a compound produced by breakdown of amino acids and lipids into an intermediate that feeds directly into the tricarboxylic acid cycle (6<\/em><\/a>). MCM uses adenosylcobalamin (AdoCbl) to generate a reactive 5\u2032-deoxyadenosyl radical (5\u2032-dA\u2022) intermediate (see the figure). In the native transformation, the enzyme carefully controls the radical, using it catalytically to abstract hydrogen (H\u2022) from a substrate methyl group. Formation of the radical enables rearrangement of the carbon skeleton, and H\u2022 is returned by the 5\u2032-dAH to allow the AdoCbl cofactor to be regenerated. This intricate choreography depends, in part, on the enzyme’s long access tunnel, which accommodates and recognizes the CoA appendage. Only when the substrate is bound does the enzyme promote 5\u2032-dA\u2022 formation.<\/p>\n Ruetz\u00a0et al.<\/em>\u00a0show that the immunometabolite I-CoA disguises itself in the active site of\u00a0Mtb<\/em>\u00a0MCM and turns the enzyme’s potent chemistry against itself, leading to an irrevocable attack on the AdoCbl cofactor. I-CoA and the native MCM substrate have nearly identical shapes. When I-CoA is bound to MCM, this similarity tricks the enzyme into forming its 5\u2032-dA\u2022 intermediate. However, ICoA directs its terminal olefin (rather than the sp3<\/sup>-hybridized carbon that, in methylmalonyl-CoA, donates H\u2022) toward 5-dA\u2022. The authors demonstrated that this feature of the\u00a0Mtb<\/em>\u00a0I-CoA complex with MCM results in radical addition to the cofactor, forming a new covalent C\u2013C bond in the active site. This permanently traps the cofactor in an inactive state. The inhibition strategy, called mechanism-based suicide inactivation, is also the basis for some of our most potent pharmaceuticals, because it minimizes off-target effects and cells can recover the affected pathway only through new enzyme synthesis.<\/p>\n Most organisms that require vitamin B12<\/sub>\u00a0use dedicated pathways to repair their cobalamin enzyme cofactors, which are difficult to synthesize and acquire (7<\/em><\/a>). Ruetz\u00a0et al.<\/em>\u00a0examined whether I-CoA\u2013inhibited MCM can be targeted by vitamin B12<\/sub>\u00a0repair machinery, which transfers the inactivated cofactor to a second protein for replacement of the deoxyadenosyl ligand and cofactor reactivation. The authors showed that I-CoA\u2013bound MCM is recognized by B12<\/sub>\u00a0repair machinery, but the inhibited enzyme does not exchange its inactivated AdoCbl for a new cofactor. Failure to deliver new cofactors to MCM can cause the repair system to break apart AdoCbl waiting to be loaded onto enzymes (8<\/em><\/a>), suggesting that itaconate could ultimately induce B12<\/sub>\u00a0deficiency in\u00a0Mtb<\/em>\u00a0(9<\/em><\/a>).<\/p>\n MCM is one of two vitamin B12<\/sub>\u00a0enzymes in humans, where it is used to prevent accumulation of toxic lipid and protein catabolites. Ruetz\u00a0et al.<\/em>\u00a0show that human MCM is also susceptible to irreversible inactivation by itaconate, raising questions about how human cells protect themselves from the immunometabolite during\u00a0Mtb<\/em>\u00a0infection. Recent work suggests that the human immune system takes additional inspiration from bacteria to shield its own B12<\/sub>\u00a0enzymes from itaconate attack. Microbes that synthesize and excrete toxic chemicals to kill neighboring cells typically produce their own internal resistance proteins. A 2017 study (9<\/em><\/a>) identified a human itaconate breakdown pathway involving an orphan enzyme, citramalyl-CoA lyase (CLYBL), in detoxification of I-CoA before it can inhibit human B12<\/sub>\u00a0enzymes. Loss of CLYBL leads to B12<\/sub>\u00a0deficiency, which is now linked by the new study to I-CoA suicide inhibition of human MCM and inactivation of human cobalamin repair pathways.\u00a0Mtb<\/em>\u00a0and other pathogens have analogous itaconate resistance pathways (10<\/em><\/a>).<\/p>\n How\u00a0Mtb<\/em>\u00a0acquires vitamin B12<\/sub>\u00a0during infection is unknown, but the pathogen might rely on host B12<\/sub>\u00a0for survival. Itaconate could affect TB disease progression through nutritional immunity, a phenomenon in which the immune system limits access to necessary transition metals for intracellular pathogens (11<\/em><\/a>). Certain human populations have a high incidence (3 to 6%) of biallelic mutations in the\u00a0CLYBL<\/em>\u00a0gene. In these individuals, loss of the human itaconate detoxification pathway and subsequent B12<\/sub>\u00a0deficiency in macrophages could further enhance the ability of the immune system to fight TB through cobalt cofactor deprivation (9<\/em><\/a>).<\/p>\n Whereas Cbl enzymes are rare, radical chemistry is common in microbes. Radical S-adenosyl-methionine (SAM) enzymes use an iron-sulfur cluster and SAM instead of AdoCbl to generate 5\u2032-dA\u2022 for aliphatic H\u2022 abstraction. Although they rely on a simpler cofactor, these more widespread bacterial proteins might be similarly vulnerable to mechanism-based 5\u2032-dA\u2022 capture by host or microbe-derived small molecules.<\/p>\n <\/p>\n <\/p>\n <\/p>\n![](\"https:\/\/science.sciencemag.org\/content\/sci\/366\/6465\/574\/F1.medium.gif\")
<\/span><\/a><\/div>\n\n
GRAPHIC: C. BICKEL\/SCIENCE<\/em><\/q><\/p>\n
![<\/i>\u00a0Download high-res image<\/span><\/a><\/li>\n<\/i>\u00a0Open in new tab<\/span><\/a><\/li>\n<\/i>\u00a0Download Powerpoint<\/span><\/a><\/li>\n<\/ul>\n<\/div>\n<\/div>ITACONATE BLOCKS A BACTERIAL B12<\/sub>\u00a0ENZYME<\/span><\/p>\nMYCOBACTERIUM TUBERCULOSIS<\/em>\u00a0(MTB<\/em>) METHYLMALONYL\u2013COENZYME A (MM-COA) MUTASE USES A LONG TUNNEL TO BIND AND ORIENT ITS NATIVE SUBSTRATE MM-COA OR THE IRREVERSIBLE INACTIVATOR ITACONYL-COA (I-COA) NEAR A VITAMIN B12<\/sub>\u2013DERIVED COFACTOR. MM-COA AND I-COA EACH TRIGGER FORMATION OF A 5\u2032-DEOXYADENOSYL (5\u2032-DA\u2022) INTERMEDIATE.<\/p>\nGRAPHIC: C. BICKEL\/SCIENCE<\/em><\/q><\/p>\n<\/div>\n<\/figcaption><\/figure>\n <\/p>\n <\/p>\nRuetz\u00a0et al.<\/em>\u00a0now address both questions by showing that I-CoA strongly inhibits\u00a0Mtb<\/em>\u00a0methylmalonyl-CoA mutase (MCM) by undergoing covalent attachment to the enzyme’s vitamin B12<\/sub>\u2013derived cobalamin (Cbl) cofactor. MCM promotes the carbon-skeleton rearrangement that converts its namesake substrate to succinyl-CoA. The reaction transforms a compound produced by breakdown of amino acids and lipids into an intermediate that feeds directly into the tricarboxylic acid cycle (6<\/em><\/a>). MCM uses adenosylcobalamin (AdoCbl) to generate a reactive 5\u2032-deoxyadenosyl radical (5\u2032-dA\u2022) intermediate (see the figure). In the native transformation, the enzyme carefully controls the radical, using it catalytically to abstract hydrogen (H\u2022) from a substrate methyl group. Formation of the radical enables rearrangement of the carbon skeleton, and H\u2022 is returned by the 5\u2032-dAH to allow the AdoCbl cofactor to be regenerated. This intricate choreography depends, in part, on the enzyme’s long access tunnel, which accommodates and recognizes the CoA appendage. Only when the substrate is bound does the enzyme promote 5\u2032-dA\u2022 formation.<\/p>\nRuetz\u00a0et al.<\/em>\u00a0show that the immunometabolite I-CoA disguises itself in the active site of\u00a0Mtb<\/em>\u00a0MCM and turns the enzyme’s potent chemistry against itself, leading to an irrevocable attack on the AdoCbl cofactor. I-CoA and the native MCM substrate have nearly identical shapes. When I-CoA is bound to MCM, this similarity tricks the enzyme into forming its 5\u2032-dA\u2022 intermediate. However, ICoA directs its terminal olefin (rather than the sp3<\/sup>-hybridized carbon that, in methylmalonyl-CoA, donates H\u2022) toward 5-dA\u2022. The authors demonstrated that this feature of the\u00a0Mtb<\/em>\u00a0I-CoA complex with MCM results in radical addition to the cofactor, forming a new covalent C\u2013C bond in the active site. This permanently traps the cofactor in an inactive state. The inhibition strategy, called mechanism-based suicide inactivation, is also the basis for some of our most potent pharmaceuticals, because it minimizes off-target effects and cells can recover the affected pathway only through new enzyme synthesis.<\/p>\nMost organisms that require vitamin B12<\/sub>\u00a0use dedicated pathways to repair their cobalamin enzyme cofactors, which are difficult to synthesize and acquire (7<\/em><\/a>). Ruetz\u00a0et al.<\/em>\u00a0examined whether I-CoA\u2013inhibited MCM can be targeted by vitamin B12<\/sub>\u00a0repair machinery, which transfers the inactivated cofactor to a second protein for replacement of the deoxyadenosyl ligand and cofactor reactivation. The authors showed that I-CoA\u2013bound MCM is recognized by B12<\/sub>\u00a0repair machinery, but the inhibited enzyme does not exchange its inactivated AdoCbl for a new cofactor. Failure to deliver new cofactors to MCM can cause the repair system to break apart AdoCbl waiting to be loaded onto enzymes (8<\/em><\/a>), suggesting that itaconate could ultimately induce B12<\/sub>\u00a0deficiency in\u00a0Mtb<\/em>\u00a0(9<\/em><\/a>).<\/p>\nMCM is one of two vitamin B12<\/sub>\u00a0enzymes in humans, where it is used to prevent accumulation of toxic lipid and protein catabolites. Ruetz\u00a0et al.<\/em>\u00a0show that human MCM is also susceptible to irreversible inactivation by itaconate, raising questions about how human cells protect themselves from the immunometabolite during\u00a0Mtb<\/em>\u00a0infection. Recent work suggests that the human immune system takes additional inspiration from bacteria to shield its own B12<\/sub>\u00a0enzymes from itaconate attack. Microbes that synthesize and excrete toxic chemicals to kill neighboring cells typically produce their own internal resistance proteins. A 2017 study (9<\/em><\/a>) identified a human itaconate breakdown pathway involving an orphan enzyme, citramalyl-CoA lyase (CLYBL), in detoxification of I-CoA before it can inhibit human B12<\/sub>\u00a0enzymes. Loss of CLYBL leads to B12<\/sub>\u00a0deficiency, which is now linked by the new study to I-CoA suicide inhibition of human MCM and inactivation of human cobalamin repair pathways.\u00a0Mtb<\/em>\u00a0and other pathogens have analogous itaconate resistance pathways (10<\/em><\/a>).<\/p>\nHow\u00a0Mtb<\/em>\u00a0acquires vitamin B12<\/sub>\u00a0during infection is unknown, but the pathogen might rely on host B12<\/sub>\u00a0for survival. Itaconate could affect TB disease progression through nutritional immunity, a phenomenon in which the immune system limits access to necessary transition metals for intracellular pathogens (11<\/em><\/a>). Certain human populations have a high incidence (3 to 6%) of biallelic mutations in the\u00a0CLYBL<\/em>\u00a0gene. In these individuals, loss of the human itaconate detoxification pathway and subsequent B12<\/sub>\u00a0deficiency in macrophages could further enhance the ability of the immune system to fight TB through cobalt cofactor deprivation (9<\/em><\/a>).<\/p>\nWhereas Cbl enzymes are rare, radical chemistry is common in microbes. Radical S-adenosyl-methionine (SAM) enzymes use an iron-sulfur cluster and SAM instead of AdoCbl to generate 5\u2032-dA\u2022 for aliphatic H\u2022 abstraction. Although they rely on a simpler cofactor, these more widespread bacterial proteins might be similarly vulnerable to mechanism-based 5\u2032-dA\u2022 capture by host or microbe-derived small molecules.<\/p>\n <\/p>\n <\/p>\n <\/p>\n(\uc6d0\ubb38: \uc5ec\uae30<\/a>\ub97c \ud074\ub9ad\ud558\uc138\uc694~)<\/p>\n <\/p>\n <\/p>\n <\/p>\n <\/p>\n","protected":false},"excerpt":{"rendered":" Microbes evolve diverse chemical strategies to survive in restrictive environments.\u00a0Mycobacterium tuberculosis\u00a0(Mtb) infection is a notable example of microbial persistence in a harsh milieu.\u00a0Mtb\u00a0causes(more…)<\/a><\/p>\n","protected":false},"author":1,"featured_media":0,"comment_status":"open","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"_monsterinsights_skip_tracking":false,"_monsterinsights_sitenote_active":false,"_monsterinsights_sitenote_note":"","_monsterinsights_sitenote_category":0,"_jetpack_newsletter_access":"","_jetpack_dont_email_post_to_subs":false,"_jetpack_newsletter_tier_id":0,"_jetpack_memberships_contains_paywalled_content":false,"_jetpack_memberships_contains_paid_content":false,"footnotes":"","jetpack_publicize_message":"","jetpack_publicize_feature_enabled":true,"jetpack_social_post_already_shared":true,"jetpack_social_options":{"image_generator_settings":{"template":"highway","default_image_id":0,"font":"","enabled":false},"version":2},"jetpack_post_was_ever_published":false},"categories":[44,38,33,29],"tags":[],"class_list":["post-4730","post","type-post","status-publish","format-standard","hentry","category-10------11--","category-38","category-do-biology","category-lets-do-science"],"aioseo_notices":[],"jetpack_publicize_connections":[],"jetpack_featured_media_url":"","jetpack-related-posts":[{"id":1366,"url":"https:\/\/biochemistry.khu.ac.kr\/lab\/?p=1366","url_meta":{"origin":4730,"position":0},"title":"Mini-tumours turn immune cells into cancer fighters","author":"biochemistry","date":"August 14, 2018","format":false,"excerpt":"\u00a0 \u00a0 (\uc6d0\ubb38) \u00a0 \u00a0 Tumour \u2018organoids\u2019 in lab dishes (left) were seeded with tissue removed from a human lung tumour (right). Credit: K. K. Dijkstra\u00a0et al.\/Cell \u00a0\u00a0 Mini-tumours turn immune cells into cancer fighters Personalized white blood cells attack tumours after incubation with cancer tissue. \u00a0 \u00a0 Miniature tumours\u2026","rel":"","context":"In "Let's Do Biology!"","block_context":{"text":"Let's Do Biology!","link":"https:\/\/biochemistry.khu.ac.kr\/lab\/?cat=33"},"img":{"alt_text":"","src":"","width":0,"height":0},"classes":[]},{"id":2451,"url":"https:\/\/biochemistry.khu.ac.kr\/lab\/?p=2451","url_meta":{"origin":4730,"position":1},"title":"Chemotherapy and tumor immunity","author":"biochemistry","date":"January 7, 2019","format":false,"excerpt":"\u00a0 \u00a0 A large increase in the incidence of cancers has been predicted for the coming years, with the number of cases worldwide rising from 15 million to 24 million between 2015 and 2035 (1). The current revolution in cancer treatment\u2014cancer immunotherapy\u2014is based on the mobilization of the immune system\u2026","rel":"","context":"In "Essays on Science"","block_context":{"text":"Essays on Science","link":"https:\/\/biochemistry.khu.ac.kr\/lab\/?cat=32"},"img":{"alt_text":"","src":"","width":0,"height":0},"classes":[]},{"id":4792,"url":"https:\/\/biochemistry.khu.ac.kr\/lab\/?p=4792","url_meta":{"origin":4730,"position":2},"title":"NGC \ucf54\uc2a4\ubaa8\uc2a4 13\ubd80\uc791 (\ub3d9\uc601\uc0c1) (\uad50\uc721\uc6a9)","author":"biochemistry","date":"May 30, 2018","format":false,"excerpt":"\u00a0 \u00a0 NGC \ucf54\uc2a4\ubaa8\uc2a4 13\ubd80\uc791 \uc911 1\ubd80 : \ud504\ub85c\ub85c\uadf8 - \uc6b0\uc8fc\uc758 \uc5ed\uc0ac \uac1c\uc694 \u00a0 \u00a0 NGC \ucf54\uc2a4\ubaa8\uc2a4 13\ubd80\uc791 \uc911 2\ubd80 : \uc0dd\uba85\uc758 \uc2e0\ube44 - \uc9c4\ud654\uc640 \uc720\uc804 \u00a0 \u00a0 NGC \ucf54\uc2a4\ubaa8\uc2a4 13\ubd80\uc791 \uc911 3\ubd80 : \ud5ec\ub9ac \ud61c\uc131, \ub274\ud2bc \u00a0 \u00a0 NGC \ucf54\uc2a4\ubaa8\uc2a4 13\ubd80\uc791 \uc911 4\ubd80 : \ube45\ubc45, \ube5b, \uc2dc\uacf5\uac04, \uc911\ub825, \ube14\ub799\ud640\u2026","rel":"","context":"In "'01. \uc6b0\uc8fc: \ubbf8\uc2dc\uc5d0\uc11c \uac70\uc2dc\uae4c\uc9c0'\uc640 '02. \uc2dc\uac04\uacfc \uacf5\uac04' \uad00\ub828"","block_context":{"text":"'01. \uc6b0\uc8fc: \ubbf8\uc2dc\uc5d0\uc11c \uac70\uc2dc\uae4c\uc9c0'\uc640 '02. \uc2dc\uac04\uacfc \uacf5\uac04' \uad00\ub828","link":"https:\/\/biochemistry.khu.ac.kr\/lab\/?cat=39"},"img":{"alt_text":"","src":"","width":0,"height":0},"classes":[]},{"id":414,"url":"https:\/\/biochemistry.khu.ac.kr\/lab\/?p=414","url_meta":{"origin":4730,"position":3},"title":"EBS \uacfc\ud559\ud601\uba85\uc758 \uc774\uc815\ud45c 5\ubd80\uc791 (\ub3d9\uc601\uc0c1) (\uad50\uc721\uc6a9)","author":"biochemistry","date":"May 30, 2018","format":false,"excerpt":"\u00a0 \u00a0 EBS \uacfc\ud559\ud601\uba85\uc758 \uc774\uc815\ud45c 5\ubd80\uc791 \uc911 1\ubd80 : \ube45\ubc45 - 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