1fqo
From Proteopedia
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{{STRUCTURE_1fqo| PDB=1fqo | SCENE= }} | {{STRUCTURE_1fqo| PDB=1fqo | SCENE= }} | ||
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===GLUCOSAMINE 6-PHOSPHATE DEAMINASE COMPLEXED WITH THE SUBSTRATE OF THE REVERSE REACTION FRUCTOSE 6-PHOSPHATE (OPEN FORM)=== | ===GLUCOSAMINE 6-PHOSPHATE DEAMINASE COMPLEXED WITH THE SUBSTRATE OF THE REVERSE REACTION FRUCTOSE 6-PHOSPHATE (OPEN FORM)=== | ||
+ | {{ABSTRACT_PUBMED_11752775}} | ||
- | + | ==Function== | |
- | + | [[http://www.uniprot.org/uniprot/NAGB_ECOLI NAGB_ECOLI]] Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.[HAMAP-Rule:MF_01241] | |
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==About this Structure== | ==About this Structure== | ||
- | [[1fqo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | [[1fqo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQO OCA]. |
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID:011752775</ref><references group="xtra"/> | + | <ref group="xtra">PMID:011752775</ref><references group="xtra"/><references/> |
- | [[Category: | + | [[Category: Bacillus coli migula 1895]] |
[[Category: Glucosamine-6-phosphate deaminase]] | [[Category: Glucosamine-6-phosphate deaminase]] | ||
[[Category: Horjales, E.]] | [[Category: Horjales, E.]] |
Revision as of 10:51, 16 April 2014
Contents |
GLUCOSAMINE 6-PHOSPHATE DEAMINASE COMPLEXED WITH THE SUBSTRATE OF THE REVERSE REACTION FRUCTOSE 6-PHOSPHATE (OPEN FORM)
Template:ABSTRACT PUBMED 11752775
Function
[NAGB_ECOLI] Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.[HAMAP-Rule:MF_01241]
About this Structure
1fqo is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA.
Reference
- Rudino-Pinera E, Morales-Arrieta S, Rojas-Trejo SP, Horjales E. Structural flexibility, an essential component of the allosteric activation in Escherichia coli glucosamine-6-phosphate deaminase. Acta Crystallogr D Biol Crystallogr. 2002 Jan;58(Pt 1):10-20. Epub 2001, Dec 21. PMID:11752775