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Article ; Online: A review of fatty acid oxidation disorder mouse models.

Babcock, Shannon J / Houten, Sander M / Gillingham, Melanie B

2024 Volume 142, Issue 1, Page(s) 108351

Abstract: Fatty acid oxidation disorders (FAODs) are a family of rare, genetic disorders that affect any part of the fatty acid oxidation pathway. Patients present with severe phenotypes, such as hypoketotic hypoglycemia, cardiomyopathy, and rhabdomyolysis, and ... ...

Abstract	Fatty acid oxidation disorders (FAODs) are a family of rare, genetic disorders that affect any part of the fatty acid oxidation pathway. Patients present with severe phenotypes, such as hypoketotic hypoglycemia, cardiomyopathy, and rhabdomyolysis, and currently manage these symptoms by the avoidance of fasting and maintaining a low-fat, high-carbohydrate diet. Because knowledge about FAODs is limited due to the small number of patients, rodent models have been crucial in learning more about these disorders, particularly in studying the molecular mechanisms involved in different phenotypes and in evaluating treatments for patients. The purpose of this review is to present the different FAOD mouse models and highlight the benefits and limitations of using these models. Specifically, we discuss the phenotypes of the available FAOD mouse models, the potential molecular causes of prominent FAOD phenotypes that have been studied using FAOD mouse models, and how FAOD mouse models have been used to evaluate treatments for patients.
Language	English
Publishing date	2024-02-23
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	1418518-0
ISSN	1096-7206 ; 1096-7192
ISSN (online)	1096-7206
ISSN	1096-7192
DOI	10.1016/j.ymgme.2024.108351
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Article ; Online: The biochemistry and physiology of long-chain dicarboxylic acid metabolism.

Ranea-Robles, Pablo / Houten, Sander M

The Biochemical journal

2023 Volume 480, Issue 9, Page(s) 607–627

Abstract: Mitochondrial β-oxidation is the most prominent pathway for fatty acid oxidation but alternative oxidative metabolism exists. Fatty acid ω-oxidation is one of these pathways and forms dicarboxylic acids as products. These dicarboxylic acids are ... ...

Abstract	Mitochondrial β-oxidation is the most prominent pathway for fatty acid oxidation but alternative oxidative metabolism exists. Fatty acid ω-oxidation is one of these pathways and forms dicarboxylic acids as products. These dicarboxylic acids are metabolized through peroxisomal β-oxidation representing an alternative pathway, which could potentially limit the toxic effects of fatty acid accumulation. Although dicarboxylic acid metabolism is highly active in liver and kidney, its role in physiology has not been explored in depth. In this review, we summarize the biochemical mechanism of the formation and degradation of dicarboxylic acids through ω- and β-oxidation, respectively. We will discuss the role of dicarboxylic acids in different (patho)physiological states with a particular focus on the role of the intermediates and products generated through peroxisomal β-oxidation. This review is expected to increase the understanding of dicarboxylic acid metabolism and spark future research.
MeSH term(s)	Microbodies/metabolism ; Fatty Acids/metabolism ; Oxidation-Reduction ; Mitochondria/metabolism ; Liver/metabolism ; Dicarboxylic Acids/metabolism ; Dicarboxylic Acids/pharmacology
Chemical Substances	Fatty Acids ; Dicarboxylic Acids
Language	English
Publishing date	2023-05-04
Publishing country	England
Document type	Review ; Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2969-5
ISSN	1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
ISSN (online)	1470-8728
ISSN	0006-2936 ; 0306-3275 ; 0264-6021
DOI	10.1042/BCJ20230041
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Article ; Online: Protein moonlighting in inborn errors of metabolism: the case of the mitochondrial acylglycerol kinase.

Houten, Sander M

Journal of inherited metabolic disease

2017 Volume 40, Issue 6, Page(s) 755–756

MeSH term(s)	Cardiomyopathies/enzymology ; Cardiomyopathies/genetics ; Cataract/enzymology ; Cataract/genetics ; Humans ; Metabolism, Inborn Errors/enzymology ; Mitochondria/enzymology ; Mitochondria/genetics ; Mitochondrial Proteins/deficiency ; Mitochondrial Proteins/genetics ; Phosphotransferases (Alcohol Group Acceptor)/deficiency ; Phosphotransferases (Alcohol Group Acceptor)/genetics
Chemical Substances	Mitochondrial Proteins ; AGK protein, human (EC 2.7.1.-) ; Phosphotransferases (Alcohol Group Acceptor) (EC 2.7.1.-)
Language	English
Publishing date	2017-09-21
Publishing country	United States
Document type	News
ZDB-ID	438341-2
ISSN	1573-2665 ; 0141-8955
ISSN (online)	1573-2665
ISSN	0141-8955
DOI	10.1007/s10545-017-0090-y
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Article ; Online: The lysine degradation pathway: Subcellular compartmentalization and enzyme deficiencies.

Leandro, João / Houten, Sander M

Molecular genetics and metabolism

2020 Volume 131, Issue 1-2, Page(s) 14–22

Abstract: Lysine degradation via formation of saccharopine is a pathway confined to the mitochondria. The second pathway for lysine degradation, the pipecolic acid pathway, is not yet fully elucidated and known enzymes are localized in the mitochondria, cytosol ... ...

Abstract	Lysine degradation via formation of saccharopine is a pathway confined to the mitochondria. The second pathway for lysine degradation, the pipecolic acid pathway, is not yet fully elucidated and known enzymes are localized in the mitochondria, cytosol and peroxisome. The tissue-specific roles of these two pathways are still under investigation. The lysine degradation pathway is clinically relevant due to the occurrence of two severe neurometabolic disorders, pyridoxine-dependent epilepsy (PDE) and glutaric aciduria type 1 (GA1). The existence of three other disorders affecting lysine degradation without apparent clinical consequences opens up the possibility to find alternative therapeutic strategies for PDE and GA1 through pathway modulation. A better understanding of the mechanisms, compartmentalization and interplay between the different enzymes and metabolites involved in lysine degradation is of utmost importance.
MeSH term(s)	Amino Acid Metabolism, Inborn Errors/genetics ; Amino Acid Metabolism, Inborn Errors/metabolism ; Amino Acid Metabolism, Inborn Errors/pathology ; Brain Diseases, Metabolic/genetics ; Brain Diseases, Metabolic/metabolism ; Brain Diseases, Metabolic/pathology ; Cytosol/metabolism ; Epilepsy/genetics ; Epilepsy/metabolism ; Epilepsy/pathology ; Glutaryl-CoA Dehydrogenase/deficiency ; Glutaryl-CoA Dehydrogenase/genetics ; Glutaryl-CoA Dehydrogenase/metabolism ; Humans ; Lysine/analogs & derivatives ; Lysine/biosynthesis ; Lysine/metabolism ; Metabolic Networks and Pathways/genetics ; Mitochondria/genetics ; Mitochondria/metabolism ; Mitochondria/pathology ; Organ Specificity/genetics ; Peroxisomes/genetics ; Peroxisomes/metabolism
Chemical Substances	Glutaryl-CoA Dehydrogenase (EC 1.3.8.6) ; Lysine (K3Z4F929H6) ; saccharopine (WBQ73O8W32)
Language	English
Publishing date	2020-07-30
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	1418518-0
ISSN	1096-7206 ; 1096-7192
ISSN (online)	1096-7206
ISSN	1096-7192
DOI	10.1016/j.ymgme.2020.07.010
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Article ; Online: Saccharopine, a lysine degradation intermediate, is a mitochondrial toxin.

Leandro, João / Houten, Sander M

The Journal of cell biology

2019 Volume 218, Issue 2, Page(s) 391–392

Abstract: Saccharopine, a nonproteinogenic amino acid originally isolated from the ... ...

Abstract	Saccharopine, a nonproteinogenic amino acid originally isolated from the yeast
MeSH term(s)	Animals ; Homeostasis ; Lysine/analogs & derivatives ; Mice ; Mitochondria ; Saccharomyces cerevisiae
Chemical Substances	Lysine (K3Z4F929H6) ; saccharopine (WBQ73O8W32)
Language	English
Publishing date	2019-01-16
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Comment
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.201901033
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Article: A case of hyperlysinemia identified by urine newborn screening.

Yeganeh, Mehdi / Auray-Blais, Christiane / Maranda, Bruno / Sabovic, Amanda / DeVita, Robert J / Lazarus, Michael B / Houten, Sander M

JIMD reports

2023 Volume 64, Issue 6, Page(s) 440–445

Abstract: Hyperlysinemia is a rare autosomal recessive deficiency of 2-aminoadipic semialdehyde synthase (AASS) affecting the initial step in lysine degradation. It is thought to be a benign biochemical abnormality, but reports on cases remain scarce. The ... ...

Abstract	Hyperlysinemia is a rare autosomal recessive deficiency of 2-aminoadipic semialdehyde synthase (AASS) affecting the initial step in lysine degradation. It is thought to be a benign biochemical abnormality, but reports on cases remain scarce. The description of additional cases, in particular, those identified without ascertainment bias, may help counseling of new cases in the future. It may also help to establish the risks associated with pharmacological inhibition of AASS, a potential therapeutic strategy that is under investigation for other inborn errors of lysine degradation. We describe the identification of a hyperlysinemia case identified in the Provincial Neonatal Urine Screening Program in Sherbrooke, Quebec. This case presented with a profile of cystinuria but with a very high increase in urinary lysine. A diagnosis of hyperlysinemia was confirmed through biochemical testing and the identification of biallelic variants in
Language	English
Publishing date	2023-10-22
Publishing country	United States
Document type	Case Reports
ZDB-ID	2672872-2
ISSN	2192-8312 ; 2192-8304
ISSN (online)	2192-8312
ISSN	2192-8304
DOI	10.1002/jmd2.12399
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Article ; Online: A novel deleterious ETFA promoter variant causative of multiple acyl-CoA dehydrogenase deficiency.

Prasun, Pankaj / Evans, Anthony / Cork, Emalyn / Houten, Sander M / Webb, Bryn D

American journal of medical genetics. Part A

2022 Volume 191, Issue 4, Page(s) 1089–1093

Abstract: Multiple acyl-CoA dehydrogenase deficiency (MADD) is an autosomal recessive disorder of fatty acid, amino acid, and choline metabolism. We describe a patient identified through newborn screening in which the diagnosis of MADD was confirmed based on ... ...

Abstract	Multiple acyl-CoA dehydrogenase deficiency (MADD) is an autosomal recessive disorder of fatty acid, amino acid, and choline metabolism. We describe a patient identified through newborn screening in which the diagnosis of MADD was confirmed based on metabolic profiling, but clinical molecular sequencing of ETFA, ETFB, and ETFDH was normal. In order to identify the genetic etiology of MADD, we performed whole genome sequencing and identified a novel homozygous promoter variant in ETFA (c.-85G > A). Subsequent studies showed decreased ETFA protein expression in lymphoblasts. A promoter luciferase assay confirmed decreased activity of the mutant promoter. In both assays, the variant displayed considerable residual activity, therefore we speculate that our patient may have a late onset form of MADD (Type III). Our findings may be helpful in establishing a molecular diagnosis in other MADD patients with a characteristic biochemical profile but apparently normal molecular studies.
MeSH term(s)	Infant, Newborn ; Humans ; Multiple Acyl Coenzyme A Dehydrogenase Deficiency/genetics ; Electron-Transferring Flavoproteins/genetics ; Amino Acids/genetics ; Homozygote ; Iron-Sulfur Proteins/genetics ; Mutation
Chemical Substances	Electron-Transferring Flavoproteins ; Amino Acids ; Iron-Sulfur Proteins ; ETFA protein, human
Language	English
Publishing date	2022-12-28
Publishing country	United States
Document type	Case Reports
ZDB-ID	2108614-X
ISSN	1552-4833 ; 0148-7299 ; 1552-4825
ISSN (online)	1552-4833
ISSN	0148-7299 ; 1552-4825
DOI	10.1002/ajmg.a.63104
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Article: Characterization, structure and inhibition of the human succinyl-CoA:glutarate-CoA transferase, a genetic modifier of glutaric aciduria type 1.

Khamrui, Susmita / Dodatko, Tetyana / Wu, Ruoxi / Leandro, João / Sabovic, Amanda / Violante, Sara / Cross, Justin R / Marsan, Eric / Kumar, Kunal / DeVita, Robert J / Lazarus, Michael B / Houten, Sander M

bioRxiv : the preprint server for biology

2024

Abstract: Glutaric Aciduria Type 1 (GA1) is a serious inborn error of metabolism with no pharmacological treatments. A novel strategy to treat this disease is to divert the toxic biochemical intermediates to less toxic or non-toxic metabolites. Here, we report a ... ...

Abstract	Glutaric Aciduria Type 1 (GA1) is a serious inborn error of metabolism with no pharmacological treatments. A novel strategy to treat this disease is to divert the toxic biochemical intermediates to less toxic or non-toxic metabolites. Here, we report a novel target, SUGCT, which we hypothesize suppresses the GA1 metabolic phenotype through decreasing glutaryl-CoA. We report the structure of SUGCT, the first eukaryotic structure of a type III CoA transferase, develop a high-throughput enzyme assay and a cell-based assay, and identify valsartan and losartan carboxylic acid as inhibitors of the enzyme validating the screening approach. These results may form the basis for future development of new pharmacological intervention to treat GA1.
Language	English
Publishing date	2024-02-07
Publishing country	United States
Document type	Preprint
DOI	10.1101/2024.02.07.578422
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Article ; Online: Metabolic interactions between peroxisomes and mitochondria with a special focus on acylcarnitine metabolism.

Houten, Sander M / Wanders, Ronald J A / Ranea-Robles, Pablo

Biochimica et biophysica acta. Molecular basis of disease

2020 Volume 1866, Issue 5, Page(s) 165720

Abstract: Carnitine plays an essential role in mitochondrial fatty acid β-oxidation as a part of a cycle that transfers long-chain fatty acids across the mitochondrial membrane and involves two carnitine palmitoyltransferases (CPT1 and CPT2). Two distinct ... ...

Abstract	Carnitine plays an essential role in mitochondrial fatty acid β-oxidation as a part of a cycle that transfers long-chain fatty acids across the mitochondrial membrane and involves two carnitine palmitoyltransferases (CPT1 and CPT2). Two distinct carnitine acyltransferases, carnitine octanoyltransferase (COT) and carnitine acetyltransferase (CAT), are peroxisomal enzymes, which indicates that carnitine is not only important for mitochondrial, but also for peroxisomal metabolism. It has been demonstrated that after peroxisomal metabolism, specific intermediates can be exported as acylcarnitines for subsequent and final mitochondrial metabolism. There is also evidence that peroxisomes are able to degrade fatty acids that are typically handled by mitochondria possibly after transport as acylcarnitines. Here we review the biochemistry and physiological functions of metabolite exchange between peroxisomes and mitochondria with a special focus on acylcarnitines.
MeSH term(s)	Carnitine/analogs & derivatives ; Carnitine/metabolism ; Carnitine Acyltransferases/metabolism ; Fatty Acids/metabolism ; Mitochondria/enzymology ; Peroxisomes/enzymology
Chemical Substances	Fatty Acids ; acylcarnitine ; Carnitine Acyltransferases (EC 2.3.1.-) ; Carnitine (S7UI8SM58A)
Language	English
Publishing date	2020-02-10
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	60-7
ISSN	1879-260X ; 1879-2596 ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-260X ; 1879-2596 ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbadis.2020.165720
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Article ; Online: Functional Versatility of the Human 2-Oxoadipate Dehydrogenase in the L-Lysine Degradation Pathway toward Its Non-Cognate Substrate 2-Oxopimelic Acid.

Nemeria, Natalia S / Nagy, Balint / Sanchez, Roberto / Zhang, Xu / Leandro, João / Ambrus, Attila / Houten, Sander M / Jordan, Frank

International journal of molecular sciences

2022 Volume 23, Issue 15

Abstract: The human 2-oxoadipate dehydrogenase complex (OADHc) in L-lysine catabolism is involved in the oxidative decarboxylation of 2-oxoadipate (OA) to glutaryl-CoA and NADH (+ ... ...

Abstract	The human 2-oxoadipate dehydrogenase complex (OADHc) in L-lysine catabolism is involved in the oxidative decarboxylation of 2-oxoadipate (OA) to glutaryl-CoA and NADH (+H
MeSH term(s)	Amino Acid Metabolism, Inborn Errors/metabolism ; Humans ; Ketoglutarate Dehydrogenase Complex/metabolism ; Lysine/metabolism ; NAD/metabolism ; Oxidation-Reduction
Chemical Substances	NAD (0U46U6E8UK) ; DHTKD1 protein, human (EC 1.2.4.2) ; Ketoglutarate Dehydrogenase Complex (EC 1.2.4.2) ; Lysine (K3Z4F929H6)
Language	English
Publishing date	2022-07-26
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms23158213
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