1e4o

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[[Image:1e4o.png|left|200px]]
 
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{{STRUCTURE_1e4o| PDB=1e4o | SCENE= }}
{{STRUCTURE_1e4o| PDB=1e4o | SCENE= }}
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===Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question===
===Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question===
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{{ABSTRACT_PUBMED_10469642}}
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==Function==
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[[http://www.uniprot.org/uniprot/PHSM_ECOLI PHSM_ECOLI]] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
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(as it appears on PubMed at http://www.pubmed.gov), where 10469642 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10469642}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:010469642</ref><references group="xtra"/>
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<ref group="xtra">PMID:010469642</ref><references group="xtra"/><references/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Phosphorylase]]
[[Category: Phosphorylase]]

Revision as of 10:30, 16 April 2014

Template:STRUCTURE 1e4o

Contents

Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question

Template:ABSTRACT PUBMED 10469642

Function

[PHSM_ECOLI] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.

About this Structure

1e4o is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

  • Watson KA, McCleverty C, Geremia S, Cottaz S, Driguez H, Johnson LN. Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question. EMBO J. 1999 Sep 1;18(17):4619-32. PMID:10469642 doi:10.1093/emboj/18.17.4619

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