4lrs

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'''Unreleased structure'''
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{{STRUCTURE_4lrs| PDB=4lrs | SCENE= }}
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===Crystal and solution structures of the bifunctional enzyme (Aldolase/Aldehyde dehydrogenase) from Thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and CoA accommodation whithin the shared cofactor-binding site===
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The entry 4lrs is ON HOLD
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==Function==
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[[http://www.uniprot.org/uniprot/D1A3K8_THECD D1A3K8_THECD]] Catalyzes the retro-aldol cleavage of 4-hydroxy-2-oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta-cleavage pathway for the degradation of aromatic compounds (By similarity).[HAMAP-Rule:MF_01656] [[http://www.uniprot.org/uniprot/D1A3K7_THECD D1A3K7_THECD]] Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds (By similarity).[HAMAP-Rule:MF_01657]
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Authors: Fischer, B., Branlant, G., Talfournier, F., Gruez, A.
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==About this Structure==
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[[4lrs]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermomonospora_curvata Thermomonospora curvata] and [http://en.wikipedia.org/wiki/Thermomonospora_curvata_dsm_43183 Thermomonospora curvata dsm 43183]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LRS OCA].
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Description: Crystal and solution structures of the bifunctional enzyme (Aldolase/Aldehyde dehydrogenase) from Thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and CoA accommodation whithin the shared cofactor-binding site
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[[Category: 4-hydroxy-2-oxovalerate aldolase]]
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[[Category: Thermomonospora curvata]]
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[[Category: Thermomonospora curvata dsm 43183]]
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[[Category: Branlant, G.]]
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[[Category: Fischer, B.]]
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[[Category: Gruez, A.]]
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[[Category: Talfournier, F.]]
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[[Category: Aldolase]]
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[[Category: Dehydrogenase]]
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[[Category: Oxidoreductase]]
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[[Category: Rossmann fold]]
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[[Category: Tim barrel domain]]

Revision as of 11:01, 4 September 2013

Template:STRUCTURE 4lrs

Crystal and solution structures of the bifunctional enzyme (Aldolase/Aldehyde dehydrogenase) from Thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and CoA accommodation whithin the shared cofactor-binding site

Function

[D1A3K8_THECD] Catalyzes the retro-aldol cleavage of 4-hydroxy-2-oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta-cleavage pathway for the degradation of aromatic compounds (By similarity).[HAMAP-Rule:MF_01656] [D1A3K7_THECD] Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds (By similarity).[HAMAP-Rule:MF_01657]

About this Structure

4lrs is a 3 chain structure with sequence from Thermomonospora curvata and Thermomonospora curvata dsm 43183. Full crystallographic information is available from OCA.

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