Sandbox Reserved 776

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(→Dehaloperoxidase)
(→Dehaloperoxidase)
Line 5: Line 5:
'''
'''
== Dehaloperoxidase ==
== Dehaloperoxidase ==
-
'''Dehaloperoxidase (DHP)''' from the marine annellid ''Amphitrite ornata'' is a dimeric enzyme weighing ~16 kDa with a heme prosthetic group and belongs to the globin family. DHP is consistent with the 'globin fold', having eight alpha helices; globins are reversible oxygen binding/transporting proteins (1). Although belonging to the globin superfamily, DHP has a biologically relevant peroxidase activity, the first known globin-peroxidase. It has previously been shown to dehalogenate trihalophenols to their corresponding dihaloquinones. Reactivity is initiated by use of H2O2 as co-substrate. [[Image:trihalophenol mech.jpg]]
+
'''Dehaloperoxidase (DHP)''' from the marine annellid ''Amphitrite ornata'' is a dimeric enzyme weighing ~16 kDa with a heme prosthetic group and belongs to the globin family. DHP is consistent with the 'globin fold', having eight alpha helices; globins are reversible oxygen binding/transporting proteins (1). Although belonging to the globin superfamily, DHP has a biologically relevant peroxidase activity, the first known globin-peroxidase. It has previously been shown to dehalogenate trihalophenols to their corresponding dihaloquinones. Reactivity is initiated by use of H2O2 as co-substrate. [[Image:trihalophenol mech.jpg]] More recent work has shown that DHP also reacts through a peroxygenase mechanism by substrate turnover with haloindoles and oxidase activity with indigo formation from 5-bromo-3-oxindole.

Revision as of 20:07, 18 November 2013

Crystal structure of DHP A with sulfate ions, 1ewa

Drag the structure with the mouse to rotate
This Sandbox is Reserved from Sep 25, 2013, through Mar 31, 2014 for use in the course "BCH455/555 Proteins and Molecular Mechanisms" taught by Michael B. Goshe at the North Carolina State University. This reservation includes Sandbox Reserved 299, Sandbox Reserved 300 and Sandbox Reserved 760 through Sandbox Reserved 779.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

Dehaloperoxidase

Dehaloperoxidase (DHP) from the marine annellid Amphitrite ornata is a dimeric enzyme weighing ~16 kDa with a heme prosthetic group and belongs to the globin family. DHP is consistent with the 'globin fold', having eight alpha helices; globins are reversible oxygen binding/transporting proteins (1). Although belonging to the globin superfamily, DHP has a biologically relevant peroxidase activity, the first known globin-peroxidase. It has previously been shown to dehalogenate trihalophenols to their corresponding dihaloquinones. Reactivity is initiated by use of H2O2 as co-substrate. Image:trihalophenol mech.jpg More recent work has shown that DHP also reacts through a peroxygenase mechanism by substrate turnover with haloindoles and oxidase activity with indigo formation from 5-bromo-3-oxindole.

Retrieved from "http://52.214.119.220/wiki/index.php/Sandbox_Reserved_776"
Personal tools