This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2nyf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2nyf.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2nyf.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2nyf| PDB=2nyf | SCENE= }}
{{STRUCTURE_2nyf| PDB=2nyf | SCENE= }}
-
'''Crystal structure of phenylalanine ammonia-lyase from Nostoc punctiforme'''
+
===Crystal structure of phenylalanine ammonia-lyase from Nostoc punctiforme===
-
==Overview==
+
<!--
-
Phenylalanine ammonia lyase (PAL) catalyzes the deamination of phenylalanine to cinnamate and ammonia. While PALs are common in terrestrial plants where they catalyze the first committed step in the formation of phenylpropanoids, only a few prokaryotic PALs have been identified to date. Here we describe for the first time PALs from cyanobacteria, in particular, Anabaena variabilis ATCC 29413 and Nostoc punctiforme ATCC 29133, identified by screening the genome sequences of these organisms for members of the aromatic amino acid ammonia lyase family. Both PAL genes associate with secondary metabolite biosynthetic gene clusters as observed for other eubacterial PAL genes. In comparison to eukaryotic homologues, the cyanobacterial PALs are 20% smaller in size but share similar substrate selectivity and kinetic activity toward L-phenylalanine over L-tyrosine. Structure elucidation by protein X-ray crystallography confirmed that the two cyanobacterial PALs are similar in tertiary and quatenary structure to plant and yeast PALs as well as the mechanistically related histidine ammonia lyases.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17240984}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17240984 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17240984}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Noel, J P.]]
[[Category: Noel, J P.]]
[[Category: Pence, J.]]
[[Category: Pence, J.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:04:35 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:23:08 2008''

Revision as of 11:23, 29 July 2008

Image:2nyf.png

Template:STRUCTURE 2nyf

Crystal structure of phenylalanine ammonia-lyase from Nostoc punctiforme

Template:ABSTRACT PUBMED 17240984

About this Structure

Full crystallographic information is available from OCA.

Reference

Discovery of two cyanobacterial phenylalanine ammonia lyases: kinetic and structural characterization., Moffitt MC, Louie GV, Bowman ME, Pence J, Noel JP, Moore BS, Biochemistry. 2007 Jan 30;46(4):1004-12. PMID:17240984

Page seeded by OCA on Tue Jul 29 14:23:08 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2nyf"
Personal tools