2012-11-28T23:18:01Z

Dami Adebambo:

{{Sandbox_Reserved_Robert_B_Rose_2}}


== '''Beta-1,4-Endoglucanase''' ==

<Structure load='3vdh' size='500' frame='true' align='right' caption='Beta-1,4-Endoglucanase' scene='Insert optional scene name here' />

Cellulose is one of the main components of the plant cell wall, found predominantly in the xylem tissue which is further protected by hemicellulose and pectin. Cellulases are enzymes that catalyze the hydrolysis of cellulose and belong to a group of enzymes termed glycoside hydrolases (GHs). Several members of the GH family demonstrate a modular architecture composed of one or two catalytic modules connected to several kinds of accessory modules (Schubot et al., 2004). The accessory modules can be involved in numerous functions. For example, some cellulases contain carbohydrate-binding modules (CBMs), which enhance the association of the catalytic modules with insoluble carbohydrates. Cellulases have been characterized as endo or exo according to their mode of action on the substrate (Parsiegla et al., 2002). The endocellulases cleave the cellulose chain at arbitrary points, while exocellulases cleave at the terminus of a chain to start the degradation process. Beta-1,4-glycosidic bonds link together the beta-D-glucopyranose units of cellulose. Beta-1-4-endoglucanase enzymes, produced chiefly by fungi, bacteria and protozoans, specifically cleave the internal bonds of the cellulose chain (Kumar et al., 2008).

[[Image:3vdh_bio_r_500.jpg | thumb]]

== '''Structure''' ==
In the past 20 years, researchers have found that endoglucanases cannot break down polysaccharides efficiently without the help of non-catalytic carbohydrate-binding modules. Thus, endoglucanase is mostly found in the form of a complex that is made up of three separate domains. The main domain contains the large, globular catalytic domain which expresses the active site. A loop of the protein chain forms a tunnel that encloses the <scene name='Sandbox_Reserved_655/Active_site/1'>active site</scene>.

This is attached at the O-glycosylated B block hinge region of the catalytic domain to the smaller, globular CBM at its C-terminal A block by a linker peptide made up of proline, serine, and threonine (Nimlos, et al., 2007).[[Image:CBM.jpg]]

The overall shape of the complex looks like a tadpole, with the A and B blocks forming the extended tail and the catalytic domain forming the head (Pilz, et al., 1990). [[Image:Quartenary.jpg]]

The CBM facilitates the enzyme by binding the complex to the cellulose, thus maintaining the proximity of the enzyme and the substrate. It can also target areas of the cellulose that are specific to the enzyme complex. In addition, the CBM itself can disrupt the structure of the cellulose and thus expose the substrate more to the enzyme. The aromatic amino acid residues and planar architecture of the CBM binding sites are complementary to the hydrophobic sites of cellulose chains (hydrophobic 110 face) (Figure 3). This exposes the beta-D-glucopyranose rings in the chair conformation, which have their alpha and beta faces having either two or three axial hydrogens exposed and ring hydroxyl groups in the equatorial position, allowing the CBMs to bind efficiently (Nimlos, et al., 2007). The thermodynamic forces that drive this interaction is controversial, but most researchers postulate that it comes from the positive entropy when the water molecules are released from the protein and ligand (Boraston, et al., 2004).

Methods for Purification:
Ammonium Sulfate Precipitation,
Ion Exchange Chromatography,
Affinity Chromatography on a column of allosteric inhibitor bound the Sepharose (6)

Methods for Solving the Structure:
single-crystal X-ray-diffraction

== '''Mechanism''' ==
NH4+ + α-ketoglutarate + NADPH + 2 H+ → glutamate + NADP+ + H2O
::[[Image:glutamatedehydrogenase.jpeg]]

The CBM "pulls up" the chain and feeds it into the catalytic domain. As aforementioned, the CBM's hydrophoic binding site of three tyrosines remains in contact with the surface throughout the reaction but can freely move translationally. The CBM undergoes a structural conformation after the substrate is in place. The fourth tyrosine (Y13) unfolds from within the CBM and forms a van der Waals interaction with the cellulose surface on the other side of the chain, thus encompassing the reducing end. While the rest of the CBM structure remains fairly rigid because of hydrogen bonds (between strand beta-3 and beta-1 and beta-2) and disulfide bridges (between beta-1 and beta-2) that maintain spacing matching that of the cellulose monomers at the binding site, the fourth tyrosine is located on the remainder of a loop of the protein and is more flexible for the induced fit (Nimlos, et al., 2007). Within the active site, Glutamine (212) acts as a catalytic nucleophile while Trypothan (40) fixes the substrate by hydrophoic interaction at the entrance of the active site tunnel. Similar to myosin and other motor proteins, the enzyme complex is driven by the hydrolysis of the glycosidic bond of cellulose (like phosphate bonds in ATP) as a source of energy for movement along their substrate (Igarashi, et al. 2009).

== '''Applications''' ==
Glutamate dehydrogenase is a mitochondrial enzyme present in the liver and can be used to determine how well the liver is functioning. Blood serum levels are measured and if levels are high it could be indicative of hepatocellular necrosis. Liver diseases in which necrosis of heptocytes are involved, such as toxic liver damage hypoxic liver disease, are characterized by high serum GDH levels. GDH is important for distinguishing between acute viral hepatitis and acute toxic liver necrosis or acute hypoxic liver disease, particularly in the case of liver damage with very high aminotransferases. GDH is measure by conducting the following reaction. (7)

::::::::GDH
a-oxoglutarate + NADH + NH4+ ---------------> glutamate + NAD+ +H2O

As NADH is oxidized, the decrease in the absorbance per minute is measured spectrophotometrically at 340nm and is proportional to the GLDH activity.

An example of this can be seen here: [https://docs.google.com/a/ncsu.edu/viewer?a=v&pid=gmail&attid=0.2&thid=13addc1ac3f18236&mt=application/pdf&url=https://mail.google.com/mail/u/0/?ui%3D2%26ik%3D5ad9b5051c%26view%3Datt%26th%3D13addc1ac3f18236%26attid%3D0.2%26disp%3Dsafe%26realattid%3Df_h998el621%26zw&sig=AHIEtbSNiAIgz_br1UY0dW534zXhAWFV4A]

== Notes ==

<references/>

(1) F.D. Schubot, I.A. Kataeva, J. Chang, A.K. Shah, L.G. Ljungdahl, J.P. Rose, B.-C. Wang. Structural basis for the exocellulase activity of the cellobiohydrolase CbhA from Clostridium thermocellum Biochemistry, 43 (2004), pp. 1163–1170

(2) G. Parsiegla, C. Reverbel, C. Tardif, H. Driguez, R. Haser. Structures of mutants of cellulase Cel48F of Clostridium cellulotyticum in complex with long hemithiocellooligosaccharides give rise to a new view of the substrate pathway during processive action
J. Mol. Biol., 375 (2008), pp. 499–510

(3) Kumar, R., Sing, S., Singh, O.V. 2008. Bioconversion of lignocellulosic biomass: biochemical and molecular perspectives. J Ind Microbiol Biotechnol. 35: 377-391.

(4) Smith, Thomas J., and Peter E. Peterson. "The Structure of Bovine Glutamate Dehydrogenase Provides Insights into the Mechanism of Allostery." Structure 7.7 (1999): 769-782. Print.

(5) Smith, Emil L, et. all. "Bovine Liver Glutamate Dehydrogenase: Tentative Amino Acid Sequence; Identification of a Reactive Lysine; Nitration of a Specific Tyrosine and Loss of Allosteric Inhibition by Guanosine Triphosphate." Proceedings of the National Academy of Sciences 67.2 (1970): 724-730. Print.

(6) Godinot, Catherine, et. all. "A Rapid and Efficient New Method of Purification of Glutamate Dehydrogenase by Affinity Chromatography on GTP-Sepharose." Analytical Biochemistry 61.1 (1974): 264-270. Print.

(7) Randox. "Glutamate Dehydrogenase (GLDH) for the Differential Diagnosis of Liver Disease." (2007): N. pag. Print.

(8) Minter, Mellisa. "Glutamate Dehydrogenase." Oxidoreductases And The Reactions They Catalyze. University Of Wisconsin-Eau Claire, 2005. Web. 08 Nov. 2012. <http://www.chem.uwec.edu/Webpapers2005/mintermm/index.html>.

(9) King, Michael. "Nitrogen Metabolism." The Medical Biochemistry Page. Themedicalbiochemistrypage.org, 2012. Web. 08 Nov. 2012. <http://themedicalbiochemistrypage.org/nitrogen-metabolism.php>.

File:Quartenary.jpg

2012-11-28T23:16:28Z

Dami Adebambo:

Sandbox Reserved 655

2012-11-28T23:12:15Z

Dami Adebambo:

{{Sandbox_Reserved_Robert_B_Rose_2}}


== '''Beta-1,4-Endoglucanase''' ==

<Structure load='3vdh' size='500' frame='true' align='right' caption='Beta-1,4-Endoglucanase' scene='Insert optional scene name here' />

Cellulose is one of the main components of the plant cell wall, found predominantly in the xylem tissue which is further protected by hemicellulose and pectin. Cellulases are enzymes that catalyze the hydrolysis of cellulose and belong to a group of enzymes termed glycoside hydrolases (GHs). Several members of the GH family demonstrate a modular architecture composed of one or two catalytic modules connected to several kinds of accessory modules (Schubot et al., 2004). The accessory modules can be involved in numerous functions. For example, some cellulases contain carbohydrate-binding modules (CBMs), which enhance the association of the catalytic modules with insoluble carbohydrates. Cellulases have been characterized as endo or exo according to their mode of action on the substrate (Parsiegla et al., 2002). The endocellulases cleave the cellulose chain at arbitrary points, while exocellulases cleave at the terminus of a chain to start the degradation process. Beta-1,4-glycosidic bonds link together the beta-D-glucopyranose units of cellulose. Beta-1-4-endoglucanase enzymes, produced chiefly by fungi, bacteria and protozoans, specifically cleave the internal bonds of the cellulose chain (Kumar et al., 2008).

[[Image:3vdh_bio_r_500.jpg | thumb]]

== '''Structure''' ==
In the past 20 years, researchers have found that endoglucanases cannot break down polysaccharides efficiently without the help of non-catalytic carbohydrate-binding modules. Thus, endoglucanase is mostly found in the form of a complex that is made up of three separate domains. The main domain contains the large, globular catalytic domain which expresses the active site. A loop of the protein chain forms a tunnel that encloses the <scene name='Sandbox_Reserved_655/Active_site/1'>active site</scene>.

This is attached at the O-glycosylated B block hinge region of the catalytic domain to the smaller, globular CBM at its C-terminal A block by a linker peptide made up of proline, serine, and threonine (Nimlos, et al., 2007).[[Image:CBM.jpg]]

The overall shape of the complex looks like a tadpole, with the A and B blocks forming the extended tail and the catalytic domain forming the head (Pilz, et al., 1990). The CBM facilitates the enzyme by binding the complex to the cellulose, thus maintaining the proximity of the enzyme and the substrate. It can also target areas of the cellulose that are specific to the enzyme complex. In addition, the CBM itself can disrupt the structure of the cellulose and thus expose the substrate more to the enzyme. The aromatic amino acid residues and planar architecture of the CBM binding sites are complementary to the hydrophobic sites of cellulose chains (hydrophobic 110 face) (Figure 3). This exposes the beta-D-glucopyranose rings in the chair conformation, which have their alpha and beta faces having either two or three axial hydrogens exposed and ring hydroxyl groups in the equatorial position, allowing the CBMs to bind efficiently (Nimlos, et al., 2007). The thermodynamic forces that drive this interaction is controversial, but most researchers postulate that it comes from the positive entropy when the water molecules are released from the protein and ligand (Boraston, et al., 2004).

Methods for Purification:
Ammonium Sulfate Precipitation,
Ion Exchange Chromatography,
Affinity Chromatography on a column of allosteric inhibitor bound the Sepharose (6)

Methods for Solving the Structure:
single-crystal X-ray-diffraction

== '''Mechanism''' ==
NH4+ + α-ketoglutarate + NADPH + 2 H+ → glutamate + NADP+ + H2O
::[[Image:glutamatedehydrogenase.jpeg]]

The CBM "pulls up" the chain and feeds it into the catalytic domain. As aforementioned, the CBM's hydrophoic binding site of three tyrosines remains in contact with the surface throughout the reaction but can freely move translationally. The CBM undergoes a structural conformation after the substrate is in place. The fourth tyrosine (Y13) unfolds from within the CBM and forms a van der Waals interaction with the cellulose surface on the other side of the chain, thus encompassing the reducing end. While the rest of the CBM structure remains fairly rigid because of hydrogen bonds (between strand beta-3 and beta-1 and beta-2) and disulfide bridges (between beta-1 and beta-2) that maintain spacing matching that of the cellulose monomers at the binding site, the fourth tyrosine is located on the remainder of a loop of the protein and is more flexible for the induced fit (Nimlos, et al., 2007). Within the active site, Glutamine (212) acts as a catalytic nucleophile while Trypothan (40) fixes the substrate by hydrophoic interaction at the entrance of the active site tunnel. Similar to myosin and other motor proteins, the enzyme complex is driven by the hydrolysis of the glycosidic bond of cellulose (like phosphate bonds in ATP) as a source of energy for movement along their substrate (Igarashi, et al. 2009).

== '''Applications''' ==
Glutamate dehydrogenase is a mitochondrial enzyme present in the liver and can be used to determine how well the liver is functioning. Blood serum levels are measured and if levels are high it could be indicative of hepatocellular necrosis. Liver diseases in which necrosis of heptocytes are involved, such as toxic liver damage hypoxic liver disease, are characterized by high serum GDH levels. GDH is important for distinguishing between acute viral hepatitis and acute toxic liver necrosis or acute hypoxic liver disease, particularly in the case of liver damage with very high aminotransferases. GDH is measure by conducting the following reaction. (7)

::::::::GDH
a-oxoglutarate + NADH + NH4+ ---------------> glutamate + NAD+ +H2O

As NADH is oxidized, the decrease in the absorbance per minute is measured spectrophotometrically at 340nm and is proportional to the GLDH activity.

An example of this can be seen here: [https://docs.google.com/a/ncsu.edu/viewer?a=v&pid=gmail&attid=0.2&thid=13addc1ac3f18236&mt=application/pdf&url=https://mail.google.com/mail/u/0/?ui%3D2%26ik%3D5ad9b5051c%26view%3Datt%26th%3D13addc1ac3f18236%26attid%3D0.2%26disp%3Dsafe%26realattid%3Df_h998el621%26zw&sig=AHIEtbSNiAIgz_br1UY0dW534zXhAWFV4A]

== Notes ==

<references/>

(1) F.D. Schubot, I.A. Kataeva, J. Chang, A.K. Shah, L.G. Ljungdahl, J.P. Rose, B.-C. Wang. Structural basis for the exocellulase activity of the cellobiohydrolase CbhA from Clostridium thermocellum Biochemistry, 43 (2004), pp. 1163–1170

(2) G. Parsiegla, C. Reverbel, C. Tardif, H. Driguez, R. Haser. Structures of mutants of cellulase Cel48F of Clostridium cellulotyticum in complex with long hemithiocellooligosaccharides give rise to a new view of the substrate pathway during processive action
J. Mol. Biol., 375 (2008), pp. 499–510

(3) Kumar, R., Sing, S., Singh, O.V. 2008. Bioconversion of lignocellulosic biomass: biochemical and molecular perspectives. J Ind Microbiol Biotechnol. 35: 377-391.

(4) Smith, Thomas J., and Peter E. Peterson. "The Structure of Bovine Glutamate Dehydrogenase Provides Insights into the Mechanism of Allostery." Structure 7.7 (1999): 769-782. Print.

(5) Smith, Emil L, et. all. "Bovine Liver Glutamate Dehydrogenase: Tentative Amino Acid Sequence; Identification of a Reactive Lysine; Nitration of a Specific Tyrosine and Loss of Allosteric Inhibition by Guanosine Triphosphate." Proceedings of the National Academy of Sciences 67.2 (1970): 724-730. Print.

(6) Godinot, Catherine, et. all. "A Rapid and Efficient New Method of Purification of Glutamate Dehydrogenase by Affinity Chromatography on GTP-Sepharose." Analytical Biochemistry 61.1 (1974): 264-270. Print.

(7) Randox. "Glutamate Dehydrogenase (GLDH) for the Differential Diagnosis of Liver Disease." (2007): N. pag. Print.

(8) Minter, Mellisa. "Glutamate Dehydrogenase." Oxidoreductases And The Reactions They Catalyze. University Of Wisconsin-Eau Claire, 2005. Web. 08 Nov. 2012. <http://www.chem.uwec.edu/Webpapers2005/mintermm/index.html>.

(9) King, Michael. "Nitrogen Metabolism." The Medical Biochemistry Page. Themedicalbiochemistrypage.org, 2012. Web. 08 Nov. 2012. <http://themedicalbiochemistrypage.org/nitrogen-metabolism.php>.

Sandbox Reserved 655

2012-11-28T23:07:06Z

Dami Adebambo:

{{Sandbox_Reserved_Robert_B_Rose_2}}


== '''Beta-1,4-Endoglucanase''' ==

<Structure load='3vdh' size='500' frame='true' align='right' caption='Beta-1,4-Endoglucanase' scene='Insert optional scene name here' />

Cellulose is one of the main components of the plant cell wall, found predominantly in the xylem tissue which is further protected by hemicellulose and pectin. Cellulases are enzymes that catalyze the hydrolysis of cellulose and belong to a group of enzymes termed glycoside hydrolases (GHs). Several members of the GH family demonstrate a modular architecture composed of one or two catalytic modules connected to several kinds of accessory modules (Schubot et al., 2004). The accessory modules can be involved in numerous functions. For example, some cellulases contain carbohydrate-binding modules (CBMs), which enhance the association of the catalytic modules with insoluble carbohydrates. Cellulases have been characterized as endo or exo according to their mode of action on the substrate (Parsiegla et al., 2002). The endocellulases cleave the cellulose chain at arbitrary points, while exocellulases cleave at the terminus of a chain to start the degradation process. Beta-1,4-glycosidic bonds link together the beta-D-glucopyranose units of cellulose. Beta-1-4-endoglucanase enzymes, produced chiefly by fungi, bacteria and protozoans, specifically cleave the internal bonds of the cellulose chain (Kumar et al., 2008).

== '''Structure''' ==
In the past 20 years, researchers have found that endoglucanases cannot break down polysaccharides efficiently without the help of non-catalytic carbohydrate-binding modules. Thus, endoglucanase is mostly found in the form of a complex that is made up of three separate domains. The main domain contains the large, globular catalytic domain which expresses the active site. A loop of the protein chain forms a tunnel that encloses the <scene name='Sandbox_Reserved_655/Active_site/1'>active site</scene>.

This is attached at the O-glycosylated B block hinge region of the catalytic domain to the smaller, globular CBM at its C-terminal A block by a linker peptide made up of proline, serine, and threonine (Nimlos, et al., 2007).[[Image:CBM.jpg]]

The overall shape of the complex looks like a tadpole, with the A and B blocks forming the extended tail and the catalytic domain forming the head (Pilz, et al., 1990). The CBM facilitates the enzyme by binding the complex to the cellulose, thus maintaining the proximity of the enzyme and the substrate. It can also target areas of the cellulose that are specific to the enzyme complex. In addition, the CBM itself can disrupt the structure of the cellulose and thus expose the substrate more to the enzyme. The aromatic amino acid residues and planar architecture of the CBM binding sites are complementary to the hydrophobic sites of cellulose chains (hydrophobic 110 face) (Figure 3). This exposes the beta-D-glucopyranose rings in the chair conformation, which have their alpha and beta faces having either two or three axial hydrogens exposed and ring hydroxyl groups in the equatorial position, allowing the CBMs to bind efficiently (Nimlos, et al., 2007). The thermodynamic forces that drive this interaction is controversial, but most researchers postulate that it comes from the positive entropy when the water molecules are released from the protein and ligand (Boraston, et al., 2004).

[[Image:3vdh_bio_r_500.jpg | thumb]]

Methods for Purification:
Ammonium Sulfate Precipitation,
Ion Exchange Chromatography,
Affinity Chromatography on a column of allosteric inhibitor bound the Sepharose (6)

Methods for Solving the Structure:
single-crystal X-ray-diffraction

== '''Mechanism''' ==
NH4+ + α-ketoglutarate + NADPH + 2 H+ → glutamate + NADP+ + H2O
::[[Image:glutamatedehydrogenase.jpeg]]

Glutamate dehydrogenase is important in nitrogen and glutamate metabolism and energy homeostasis. In the reaction above the forward reaction is essential in converting free ammonia and α-ketoglutarate to glutamate, an amino acid that is used for protein synthesis. The reverse reaction is key reaction that links amino acid metabolism with the Tricarboxylic Acid cycle (TCA cycle). Both reactions utilize nicotinamide nucleotide cofactors: NAD+ when nitrogen is released and NADPH when nitrogen is used. Glutamate dehydrogenase is regulated by cell energy charge. This requires Adenosine triphosphate (ATP) and Guanosine triphosphate (GTP) are positive allosteric effectors for the forward reaction and Adenosine diphosphate (ADP) and Guanosine diphosphate are positive allosteric effectors for the reverse reaction. When the level of ATP is high, conversion of glutamate to α-ketoglurate and other TCA cycle intermediates is limited; when the cellular energy charge is low, glutamate is converted to ammonia and oxidizable TCA cycle intermediates. Glutamate is an important amino acid since it gives an amine group for many transamination reactions, thus, glutamate dehydrogenase is essential in producing this amino acid. (9)

== '''Applications''' ==
Glutamate dehydrogenase is a mitochondrial enzyme present in the liver and can be used to determine how well the liver is functioning. Blood serum levels are measured and if levels are high it could be indicative of hepatocellular necrosis. Liver diseases in which necrosis of heptocytes are involved, such as toxic liver damage hypoxic liver disease, are characterized by high serum GDH levels. GDH is important for distinguishing between acute viral hepatitis and acute toxic liver necrosis or acute hypoxic liver disease, particularly in the case of liver damage with very high aminotransferases. GDH is measure by conducting the following reaction. (7)

::::::::GDH
a-oxoglutarate + NADH + NH4+ ---------------> glutamate + NAD+ +H2O

As NADH is oxidized, the decrease in the absorbance per minute is measured spectrophotometrically at 340nm and is proportional to the GLDH activity.

An example of this can be seen here: [https://docs.google.com/a/ncsu.edu/viewer?a=v&pid=gmail&attid=0.2&thid=13addc1ac3f18236&mt=application/pdf&url=https://mail.google.com/mail/u/0/?ui%3D2%26ik%3D5ad9b5051c%26view%3Datt%26th%3D13addc1ac3f18236%26attid%3D0.2%26disp%3Dsafe%26realattid%3Df_h998el621%26zw&sig=AHIEtbSNiAIgz_br1UY0dW534zXhAWFV4A]

== Notes ==

<references/>

(1) F.D. Schubot, I.A. Kataeva, J. Chang, A.K. Shah, L.G. Ljungdahl, J.P. Rose, B.-C. Wang. Structural basis for the exocellulase activity of the cellobiohydrolase CbhA from Clostridium thermocellum Biochemistry, 43 (2004), pp. 1163–1170

(2) G. Parsiegla, C. Reverbel, C. Tardif, H. Driguez, R. Haser. Structures of mutants of cellulase Cel48F of Clostridium cellulotyticum in complex with long hemithiocellooligosaccharides give rise to a new view of the substrate pathway during processive action
J. Mol. Biol., 375 (2008), pp. 499–510

(3) Kumar, R., Sing, S., Singh, O.V. 2008. Bioconversion of lignocellulosic biomass: biochemical and molecular perspectives. J Ind Microbiol Biotechnol. 35: 377-391.

(4) Smith, Thomas J., and Peter E. Peterson. "The Structure of Bovine Glutamate Dehydrogenase Provides Insights into the Mechanism of Allostery." Structure 7.7 (1999): 769-782. Print.

(5) Smith, Emil L, et. all. "Bovine Liver Glutamate Dehydrogenase: Tentative Amino Acid Sequence; Identification of a Reactive Lysine; Nitration of a Specific Tyrosine and Loss of Allosteric Inhibition by Guanosine Triphosphate." Proceedings of the National Academy of Sciences 67.2 (1970): 724-730. Print.

(6) Godinot, Catherine, et. all. "A Rapid and Efficient New Method of Purification of Glutamate Dehydrogenase by Affinity Chromatography on GTP-Sepharose." Analytical Biochemistry 61.1 (1974): 264-270. Print.

(7) Randox. "Glutamate Dehydrogenase (GLDH) for the Differential Diagnosis of Liver Disease." (2007): N. pag. Print.

(8) Minter, Mellisa. "Glutamate Dehydrogenase." Oxidoreductases And The Reactions They Catalyze. University Of Wisconsin-Eau Claire, 2005. Web. 08 Nov. 2012. <http://www.chem.uwec.edu/Webpapers2005/mintermm/index.html>.

(9) King, Michael. "Nitrogen Metabolism." The Medical Biochemistry Page. Themedicalbiochemistrypage.org, 2012. Web. 08 Nov. 2012. <http://themedicalbiochemistrypage.org/nitrogen-metabolism.php>.

2012-11-28T20:42:43Z

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