Sandbox 48: Difference between revisions
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== Adenylate Kinase == | == Adenylate Kinase == | ||
Adenylate kinase (or ADK) is an enzyme known to catalyze the interconversion of adenosine triphosphate (ATP) and adenosine monophosphate (AMP) to two molecules of adenosine diphosphate (ADP) | |||
<scene name='Sandbox_48/Full_adenylate_kinase/1'>Adenylate kinase</scene> (or ADK) is an enzyme known to catalyze the reversible interconversion of adenosine triphosphate (ATP) and adenosine monophosphate (AMP) to two molecules of adenosine diphosphate (ADP). | |||
Reaction Scheme: ATP + AMP ⇔ 2 ADP | |||
This enzyme is important for cellular energy homeostasis because the need for ADP. ADP is required for oxidative phosphorylation, an important step in multiple metabolic pathways. | |||
== Secondary Structure & Hydrogen Bonds == | == Secondary Structure & Hydrogen Bonds == | ||
The structure of <scene name='Sandbox_48/Adenylate_kinase__chain_a/1'>chain A in adenylate kinase</scene> demonstrates the types of secondary structure that make up the enzyme. | |||
The <scene name='Sandbox_48/Secondary__structure__greenblu/4'>secondary structures</scene> of chain A of adenylate kinase includes alpha- | |||
<scene name='Sandbox_48/Secondary__structure__helix/1'>helices</scene> (green), and <scene name='Sandbox_48/Secondary__structure__betashee/1'>beta sheets</scene> (blue). There are 12 total helices in the enzyme, and 2 types of | |||
beta sheets, a parallel with 5 strands and an antiparallel with 2 strands. The location of the <scene name='Sandbox_48/2_structure_hbondson/1'>hydrogen bonds</scene> (black) within the secondary structure demonstrates how the alpha-helices and beta-sheets are hydrogen bonded. | |||
== Hydrophobic and Hydrophilic Residues == | == Hydrophobic and Hydrophilic Residues == | ||
