Interactive Quiz on
Amino Acid Catabolism (N)
Reading:
Textbook Reading: Voet & Voet, Biochemistry, 3rd Edition, p. 985-995.
Some recent articles
(optional reading):
G. Schneider, H. Käck & Y. Lindqvist (2000)
"The manifold of vitamin B6 dependent enzymes," Structure 8: R1-R6.
X. Huang, H. M. Holden & F. M. Raushel (2001) "Channeling of substrates and
intermediates in enzyme-catalyzed reactions," Annu. Rev. Biochem 70: 149-180.
S. M. Morris (2002) "Regulation of enzymes of the urea cycle and arginine
metabolism," Annu. Rev. Nutr. 22: 87-105.
H. Hayashi, H. Mizuguchi, I. Miyahara, M. M. Islam, H. Ikushiro, Y. Nakajima, K.
Hirotsu & H. Kagamiyama (2003) "Strain and catalysis in aspartate
aminotransferase," Biochim. Biophys. Acta 1647: 103-109.
L. Caldovic & M. Tuchman (2003) "N-Acetylglutamate and its changing role
through evolution," Biochem. J. 372: 279-290.
A. Husson, C. Brasse-Lagnel, A. Fairand, S. Renouf & A. Lavoinne (2003)
"Argininosuccinate synthetase from the urea cycle to the citrulline-NO cycle,"
Eur. J. Biochem. 270: 1887-1899.
J. Jänne, L. Alhonen, M. Pietilä
& T. A. Keinänen (2004) "Genetic approaches
to the cellular functions of polyamines in mammals," Eur. J. Biochem. 271:
877-894.
D. J. Stuehr, J. Santolini, Z.-Q. Wang, Chin-Chuan Wei & S. Adak (2004) "Update
on mechanism and catalytic regulation in the NO synthases," J. Biol. Chem. 279:
36167-36170.
B.-Y. Hwang, B.-K. Cho, H. Yun, K. Koteshwar & B.-G. Kim (2005) "Revisit of
aminotransferase in the genomic era and its application to biocatalysis," J.
Molec. Catalysis B: Enzymatic 37: 47-55.
B. Gyorgy, E. Toth, E. Tarcsa, A. Falus & E. I. Buzas (2006) "Citrullination: A
posttranslational modification in health and disease," Internat. J. Biochem &
Cell Biol. 38: 1662-1677.
S. Lamas, C. J. Lowenstein & T. Michel (2007) "Nitric oxide signaling comes of
age: 20 years and thriving," Cardiovascular Res. 75: 207-209 (and accompanying
articles).
A. C. F. Gorren & B. Mayer (2007) Nitric-oxide synthase: A cytochrome P450
family foster child," Biochim. Biophys. Acta 1770: 432-445.
P. Pacher, J. S. Beckman & L. Liaudet (2007) "Nitric oxide and peroxynitrite in
health and disease," Physiol. Rev. 87: 315-424.
T. Kuhara (2007) "Noninvasive human metabolome analysis for differential
diagnosis of inborn errors of metabolism," J. Chromatography B 855: 42-50.
1. Write out the reactions by which the transaminase (aminotransferase) and glutamate dehydrogenase enzymes work together to deaminate amino acids consumed in excess of nutritional needs. Include structures of substrates and products of both reactions, using a specific example for the transaminase reaction.
2.a. Write out the individual steps of the reaction catalyzed by the mitochondrial enzyme Carbamoyl
Phosphate Synthase I, giving names and structures of reactants and products for each of the three steps. (Structure of ATP
may be omitted.)
b. What compound causing mental retardation is elevated
in the blood if this enzyme is inadequate? How might hereditary deficiency of
Carbamoyl Phosphate Synthase be treated? Explain.
3. Diagram and describe the reaction sequence during catalysis by transaminase (aminotransferase) enzyme, including structures of different forms of the active site cofactor, substrates and products. For your diagrams, assume that alanine is the amino group donor and a-ketoglutarate is the acceptor.
Copyright © 1998-2008 by Joyce J. Diwan. All rights reserved.
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