Sandbox Reserved 795
From Proteopedia
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<Structure load='1u8f' size='500' frame='true' align='right' caption='Glyceraldehyde-3-phosphate dehydrogenase' scene='Insert optional scene name here' /> | <Structure load='1u8f' size='500' frame='true' align='right' caption='Glyceraldehyde-3-phosphate dehydrogenase' scene='Insert optional scene name here' /> | ||
| - | <scene name='56/563207/G-3-p_dehydrogenase/3'>Glyceraldehyde 3-phosphate dehydrogenase</scene> , or G-3-P dehydrogenase, is an enzyme that plays a significant role in metabolism. It catalyzes a step in glycolysis in which glyceraldehyde 3-phosphate is converted to 3-phospho-D-glyceroyl phosphate. G-3-P dehydrogenase is a tetramer protein made up of four subunits. The <scene name='56/563207/Secondary_structure/2'>secondary structure</scene> of G-3-P dehydrogenase consists of alpha helices which are displayed in yellow and beta sheets which are displayed in pink. The majority of the beta sheets are parallel, however there are some | + | <scene name='56/563207/G-3-p_dehydrogenase/3'>Glyceraldehyde 3-phosphate dehydrogenase</scene> , or G-3-P dehydrogenase, is an enzyme that plays a significant role in metabolism. It catalyzes a step in glycolysis in which glyceraldehyde 3-phosphate is converted to 3-phospho-D-glyceroyl phosphate. This particular enzyme is human placental G-3-P dehydrogenase. It is a tetramer protein made up of four subunits. The <scene name='56/563207/Secondary_structure/2'>secondary structure</scene> of G-3-P dehydrogenase consists of alpha helices which are displayed in yellow and beta sheets which are displayed in pink. The majority of the beta sheets are parallel, however there are some antiparallel sheets as well. It seems as though the majority of the alpha helices are located around the outside of the enzyme, suggesting that they are made up of polar or charged amino acids that will interact with the hydrophilic environment. |
==Hydrogen Bonds== | ==Hydrogen Bonds== | ||
Revision as of 04:49, 15 October 2013
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| This Sandbox is Reserved from Oct 10, 2013, through May 20, 2014 for use in the course "CHEM 410 Biochemistry 1 and 2" taught by Hanna Tims at the Messiah College. This reservation includes Sandbox Reserved 780 through Sandbox Reserved 807. |
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Introduction and General Structure
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, or G-3-P dehydrogenase, is an enzyme that plays a significant role in metabolism. It catalyzes a step in glycolysis in which glyceraldehyde 3-phosphate is converted to 3-phospho-D-glyceroyl phosphate. This particular enzyme is human placental G-3-P dehydrogenase. It is a tetramer protein made up of four subunits. The of G-3-P dehydrogenase consists of alpha helices which are displayed in yellow and beta sheets which are displayed in pink. The majority of the beta sheets are parallel, however there are some antiparallel sheets as well. It seems as though the majority of the alpha helices are located around the outside of the enzyme, suggesting that they are made up of polar or charged amino acids that will interact with the hydrophilic environment.
Hydrogen Bonds
The of the backbone is displayed in black. Hydrogen bonding helps to stabilize the structure. Where the beta sheets are parallel, the hydrogen bonds are slanted. Where the beta sheets are antiparallel, the hydrogen bonds are straight. There are no disulfide bonds present in this enzyme.
