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Metabolism of amino acids - exercise - Vladimíra Kvasnicová Choose essential amino acids a) Asp, Glu b) Val, Leu, Ile c) Ala, Ser, Gly d) Phe, Trp Choose essential amino acids a) Asp, Glu b) Val, Leu, Ile c) Ala, Ser, Gly d) Phe, Trp Essential amino acids „10“ 1) branched chain: Val, Leu, Ile 2) basic: His, Arg, Lys 3) aromatic: Phe (→ Tyr), 4) sulfur-containing: Met (→ Cys) 5) other: Thr Trp Choose amino acids from which the other amino acid can be synthesized in a human body a) valine → leucine b) aspartate → asparagine c) phenylalanine → tyrosine d) methionine + serine → cysteine Choose amino acids from which the other amino acid can be synthesized in a human body a) valine → leucine leucine is the essential AA b) aspartate → asparagine c) phenylalanine → tyrosine d) methionine + serine → cysteine Synthesis of ASPARAGINE needs glutamine as –NH2 group donor (it is not ammonia as in the Gln synthesis) The figure was adopted from Devlin, T. M. (editor): Textbook of Biochemistry with Clinical Correlations, 4th ed. Wiley-Liss, Inc., New York, 1997. ISBN 0-471-15451-2 Synthesis of Tyr from Phe The figure is from http://web.indstate.edu/thcme/mwking/amino-acid-metabolism.html (Jan 2007) Synthesis of Cys from Met and Ser The figure is from http://web.indstate.edu/thcme/mwking/amino-acid-metabolism.html (Jan 2007) The amino acids can be formed from the citrate cycle intermediates in a human body a) -ketoglutarate → glutamate b) succinyl-CoA → isoleucine c) oxaloacetate → aspartate d) malate → threonine The amino acids can be formed from the citrate cycle intermediates in a human body a) -ketoglutarate → glutamate b) succinyl-CoA → isoleucine Ile is the essential AA c) oxaloacetate → aspartate d) malate → threonine Thr is the essential AA Amphibolic character of citrate cycle The figure is from http://www.tcd.ie/Biochemistry/IUBMB-Nicholson/gif/13.html (Dec 2006) The compound(s) can be synthesized from the amino acid a) tyrosine → serotonin b) serine → ethanolamine c) tryptophan → catecholamines d) cysteine → taurine The compound(s) can be synthesized from the amino acid a) tyrosine → serotonin Tyr → catecholamines b) serine → ethanolamine formed by decarboxylation c) tryptophan → catecholamines d) cysteine → taurine Trp → serotonin taurin is used in conjugation reactions in the liver – it is bound to hydrophobic substances to increase their solubility (e.g. conjugation of bile acids) The figure was adopted from Devlin, T. M. (editor): Textbook of Biochemistry with Clinical Correlations, 4th ed. Wiley-Liss, Inc., New York, 1997. ISBN 0-471-15451-2 If the amino acid is metabolised the substance is formed: a) methionine gives homocysteine b) serine gives glycine and folic acid derivative: methylene tetrahydrofolate c) glutamine releases ammonia d) some amino acides can be degraded to acetoacetate If the amino acid is metabolised the substance is formed: a) methionine gives homocysteine b) serine gives glycine and folic acid derivative: methylene tetrahydrofolate c) glutamine releases ammonia d) some amino acides can be degraded to acetoacetate = one of ketone bodies Regeneration of Met B12 (vitamins: folate+B12) The figure is from http://web.indstate.edu/thcme/mwking/amino-acid-metabolism.html (Jan 2007) glycolysis Synthesis of serine and glycine The figure is from http://www.biocarta.com/pathfiles/GlycinePathway.asp (Jan 2007) Choose products of the transamination reactions a) alanine → pyruvate b) glutamate → 2-oxoglutarate c) aspartate → oxaloacetate d) phenylalanine → tyrosine Choose products of the transamination reactions a) alanine → pyruvate b) glutamate → 2-oxoglutarate c) aspartate → oxaloacetate d) phenylalanine → tyrosine it is not transamination Transamination reaction ! REVERSIBLE ! enzymes: amino transferases coenzyme: pyridoxal phosphate (vit. B6 derivative) The figure is from http://web.indstate.edu/thcme/mwking/nitrogen-metabolism.html (Jan 2007) Amino transferases important in medicine („transaminases“) alanine aminotransferase (ALT = GPT) aspartate aminotransferase (AST = GOT) The figure was adopted from Devlin, T. M. (editor): Textbook of Biochemistry with Clinical Correlations, 4th ed. Wiley-Liss, Inc., New York, 1997. ISBN 0-471-15451-2 Amino nitrogen released from carbon sceletons of AAs can be transported in blood as a) NH4+ b) alanine c) glutamine d) urea Amino nitrogen released from carbon sceletons of AAs can be transported in blood as a) NH4+ physiologically up to 35 µmol/l (NH3 + H + b) alanine formed by transamination from pyruvate c) glutamine d) urea NH4+) the most important transport form of –NH2 it is the end product of degradation of amino nitrogen (liver → kidneys → urine) Transport of amino nitrogen from degraded muscle proteins products excreted with urine The figure was adopted from Devlin, T. M. (editor): Textbook of Biochemistry with Clinical Correlations, 4th ed. Wiley-Liss, Inc., New York, 1997. ISBN 0-471-15451-2 Glucose-alanine cycle alanine transfers both the carbon sceleton for gluconeogenesis and –NH2 group The figure was adopted from Devlin, T. M. (editor): Textbook of Biochemistry with Clinical Correlations, 4th ed. Wiley-Liss, Inc., New York, 1997. ISBN 0-471-15451-2 GLUTAMINE = the most important transport form af amino nitrogen in blood glutamine synthetase it transfers two amino groups released by degradation of AAs The figure was adopted from Devlin, T. M. (editor): Textbook of Biochemistry with Clinical Correlations, 4th ed. Wiley-Liss, Inc., New York, 1997. ISBN 0-471-15451-2 Choose glucogenic amino acids a) alanine b) lysine c) leucine d) glutamine Choose glucogenic amino acids a) alanine b) lysine c) leucine d) glutamine 7 degradation products of AAs 1. pyruvate Gly, Ala, Ser, Thr, Cys, Trp 2. oxaloacetate Asp, Asn 3. -ketoglutarate Glu, Gln, Pro, Arg, His 4. succinyl-CoA Val, Ile, Met, Thr 5. fumarate Phe, Tyr 6. acetyl-CoA Ile glucogenic AAs ketogenic AAs 7. acetoacetyl-CoA Lys, Leu, Phe, Tyr, Trp Glutamate dehydrogenase (GMD) a) catalyzes conversion of Glu to oxaloacetate b) is found in mitochondria of hepatocytes c) produces ammonia d) needs pyridoxal phosphate as a coenzyme Glutamate dehydrogenase (GMD) a) catalyzes conversion of Glu to oxaloacetate b) is found in mitochondria of hepatocytes c) produces ammonia d) needs pyridoxal phosphate as a coenzyme GLUTAMATE DEHYDROGENASE removes amino group from carbon sceleton of Glu in the liver 1. –NH2 from AAs was transfered by transamination → Glu 2. free ammonia is released by oxidative deamination of Glu The figure is from http://web.indstate.edu/thcme/mwking/nitrogen-metabolism.html (Jan 2007) Choose correct statement(s) about metabolism of amino acids a) alanine aminotransferase (ALT) transforms pyruvate to alanine b) aspartate aminotransferase (AST) transforms aspartate to -ketoglutarate c) glutamine synthetase transforms glutamate to glutamine d) glutaminase catylyzes conversion of glutamine to ammonia and -ketoglutarate Choose correct statement(s) about metabolism of amino acids a) alanine aminotransferase (ALT) transforms pyruvate to alanine b) aspartate aminotransferase (AST) transforms aspartate to -ketoglutarate c) glutamine synthetase transforms glutamate to glutamine d) glutaminase catylyzes conversion of glutamine to ammonia and -ketoglutarate Amino transferases important in medicine („transaminases“) alanine aminotransferase (ALT = GPT) aspartate aminotransferase (AST = GOT) The figure was adopted from Devlin, T. M. (editor): Textbook of Biochemistry with Clinical Correlations, 4th ed. Wiley-Liss, Inc., New York, 1997. ISBN 0-471-15451-2 Glutamine is principal transport form of amino nitrogen The figure is from http://www.sbuniv.edu/~ggray/CHE3364/b1c25out.html (Dec 2006) The amino acids can enter the citrate cycle as the molecules a) alanine → → acetyl-CoA b) aspartate → oxaloacetate c) valine → → succinyl-CoA d) glutamine → → -ketoglutarate The amino acids can enter the citrate cycle as the molecules a) alanine → → acetyl-CoA b) aspartate → oxaloacetate c) valine → → succinyl-CoA d) glutamine → → -ketoglutarate The entrance of amino acids into the citrate cycle The figure is from http://www.biocarta.com/pathfiles/glucogenicPathway.asp (Jan 2007) Ornithine cycle a) proceeds only in the liver b) produces uric acid c) includes arginine as an intermediate d) produces energy in a form of ATP Ornithine cycle a) proceeds only in the liver b) produces uric acid c) includes arginine as an intermediate d) produces energy in a form of ATP Detoxication of ammonia in the liver The figure is from http://www.biocarta.com/pathfiles/ureacyclePathway.asp (Jan 2007) Interconnection of the urea cycle with the citrate cycle The figure is from http://courses.cm.utexas.edu/archive/Spring2002/CH339K/Robertus/overheads-3/ch18_TCA-Urea_link.jpg (Jan 2007) In the urea synthesis a) ammonia reacts with ornithine → citrulline b) carbamoyl phosphate synthetase I (= mitochondrial) regulates the cycle c) aspartate is used as a –NH2 group donor d) urea is formed – it can be used as an energy substrate for extrahepatic tissues In the urea synthesis a) ammonia reacts with ornithine → citrulline b) carbamoyl phosphate synthetase I (= mitochondrial) regulates the cycle c) aspartate is used as a –NH2 group donor d) urea is formed – it can be used as an energy substrate for extrahepatic tissues Regulation of urea cycle allosteric regulation + enzyme induction by protein rich diet or by metabolic changes during starvation regulatory enzyme activation carbamoyl phosphate synthetase I (= mitochondrial) N-acetylglutamate N-acetylglutamate synthetase arginine Urea synthesis is inhibited by acidosis – HCO3- is saved inhibition