M1 - Renal, Fall 2007
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1 University of Michigan Deep Blue deepblue.lib.umich.edu M1 - Renal, Fall 2007 Lyons, R.; Burney, R. Lyons, R., Burney, R. (2008, August 07). Renal. Retrieved from Open.Michigan - Educational Resources Web site: <
2 Unless otherwise noted, the content of this course material is licensed under a Creative Commons Attribution Share Alike 3.0 License. Copyright 2007, Robert Lyons. The following information is intended to inform and educate and is not a tool for self-diagnosis or a replacement for medical evaluation, advice, diagnosis or treatment by a healthcare professional. You should speak to your physician or make an appointment to be seen if you have questions or concerns about this information or your medical condition. You assume all responsibility for use and potential liability associated with any use of the material. Material contains copyrighted content, used in accordance with U.S. law. Copyright holders of content included in this material should contact open.michigan@umich.edu with any questions, corrections, or clarifications regarding the use of content. The Regents of the University of Michigan do not license the use of third party content posted to this site unless such a license is specifically granted in connection with particular content objects. Users of content are responsible for their compliance with applicable law. Mention of specific products in this recording solely represents the opinion of the speaker and does not represent an endorsement by the University of Michigan. Viewer discretion advised: Material may contain medical images that may be disturbing to some viewers.
3 Nitrogen Metabolism (and Related Topics) Amino Acid Metabolism (Nitrogen metabolism) Folate Metabolism ( One-Carbon pathways ) Nucleotide Metabolism Dr. Robert Lyons Assistant Professor, Biological Chemistry Director, DNA Sequencing Core
4 There are also PDF s of class handouts with supplemental information available in the table of contents for this course. Supplementary study material on the Web:
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6 Protein Degradation: Endogenous proteins degrade continuously - Damaged - Mis-folded - Un-needed Dietary protein intake - mostly degraded Nitrogen Balance - expresses the patient s current status - are they gaining or losing net Nitrogen?
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8 Transfer the amine back to an acceptor α-keto acid
9 In peripheral tissues, transaminases tend to form Glutamate when they catabolize amino acids In other words, alpha-ketoglutarate is the preferred acceptor, and Glutamate is the resulting amino acid: Some amino acid + α-ketoglutarate some alpha keto acid + Glutamate
10 Glutamate can donate its amines to form other amino acids as needed A specific example - production of Aspartate in liver (described a few slides from now): Glutamate + oxaloacetate α-ketoglutarate + aspartate
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12 Ammonia can also be formed by the glutamate dehydrogenase reaction and several other reactions as well.
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25 Complicating the picture: Other tissues may be involved
26 Why is Ammonia Toxic?
27 Why is Ammonia Toxic? Possible neurotoxic effects on glutamate levels (and also GABA) (due to shifting equilibria of reactions involving these compounds)
28 Why is Ammonia Toxic? Possible neurotoxic effects on glutamate levels (and also GABA) (due to shifting equilibria of reactions involving these compounds) Possible metabolic/energetics effects: - alpha-ketoglutarate levels - glutamate levels - glutamine
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30 Inherited Defects of Urea Cycle Enzymes: Diagnosis
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34 Clinical Management of Urea Cycle Defects Dialysis to remove ammonia Provide the patient with alternative ways to excrete nitrogenous compounds: * Intravenous sodium benzoate or phenylacetate * Supplemental arginine Levulose - acidifies the gut Low protein diet
35 Degrading the Amino Acid Carbon Backbone
36 Easily-degraded products after transamination: We also already know how to degrade Glutamine: glutaminase Glutamine > glutamate + ammonia and by analogy, how to degrade Asparagine: asparaginase Asparagine > aspartate + ammonia
37 Amino Acids are categorized as Glucogenic or ketogenic or both. Many amino acids are purely glucogenic: Glutamate, aspartate, alanine, glutamine, asparagine, Some amino acids are both gluco- and ketogenic: Threonine, isoleucine, phenylalanine, tyrosine, tryptophan The only PURELY ketogenic Amino Acids : leucine, lysine
38 Amino acids with 5-carbon backbones tend to form α ketoglutarate
39 Degradation and Biosynthesis of Serine and Glycine
40 Methionine Cycle And Biological Methyl Groups
41 Deficiency: Alkaptonuria Ochronosis
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44 Synthesis of Bioactive Amines
45 Synthesis of Bioactive Amines
46 NON-Essential Amino Acids: Glutamate, aspartate, alanine, glutamine, asparagine, (proline), glycine, serine (cysteine, tyrosine) Essential Amino Acids: Arginine (!), phenylalanine, methionine, histidine, Isoleucine, leucine, valine, threonine, tryptophan, lysine
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