1nrg: Difference between revisions

Revision as of 04:45, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1nrg.png

Template:STRUCTURE 1nrg

Structure and Properties of Recombinant Human Pyridoxine-5'-Phosphate OxidaseStructure and Properties of Recombinant Human Pyridoxine-5'-Phosphate Oxidase

Template:ABSTRACT PUBMED 12824491

About this StructureAbout this Structure

1NRG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structure and properties of recombinant human pyridoxine 5'-phosphate oxidase., Musayev FN, Di Salvo ML, Ko TP, Schirch V, Safo MK, Protein Sci. 2003 Jul;12(7):1455-63. PMID:12824491

Page seeded by OCA on Tue Jul 29 04:45:06 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1nrg.jpg|left|200px]]
+{{Seed}}
+[[Image:1nrg.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1nrg|  PDB=1nrg  |  SCENE=  }}
-'''Structure and Properties of Recombinant Human Pyridoxine-5'-Phosphate Oxidase'''
+===Structure and Properties of Recombinant Human Pyridoxine-5'-Phosphate Oxidase===
-==Overview==
+<!--
-Pyridoxine 5'-phosphate oxidase catalyzes the terminal step in the synthesis of pyridoxal 5'-phosphate. The cDNA for the human enzyme has been cloned and expressed in Escherichia coli. The purified human enzyme is a homodimer that exhibits a low catalytic rate constant of approximately 0.2 sec(-1) and K(m) values in the low micromolar range for both pyridoxine 5'phosphate and pyridoxamine 5'-phosphate. Pyridoxal 5'-phosphate is an effective product inhibitor. The three-dimensional fold of the human enzyme is very similar to those of the E. coli and yeast enzymes. The human and E. coli enzymes share 39% sequence identity, but the binding sites for the tightly bound FMN and substrate are highly conserved. As observed with the E. coli enzyme, the human enzyme binds one molecule of pyridoxal 5'-phosphate tightly on each subunit.
+The line below this paragraph, {{ABSTRACT_PUBMED_12824491}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12824491 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12824491}}
 ==About this Structure==
@@ Line 31: / Line 35: @@
 [[Category: Plp]]
 [[Category: Pyridoxine-5'-phosphate]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:53:38 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:45:06 2008''