1ald
From Proteopedia
(New page: 200px<br /> <applet load="1ald" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ald, resolution 2.0Å" /> '''ACTIVITY AND SPECIFI...) |
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| - | [[Image:1ald.gif|left|200px]]<br /> | + | [[Image:1ald.gif|left|200px]]<br /><applet load="1ald" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1ald, resolution 2.0Å" /> | caption="1ald, resolution 2.0Å" /> | ||
'''ACTIVITY AND SPECIFICITY OF HUMAN ALDOLASES'''<br /> | '''ACTIVITY AND SPECIFICITY OF HUMAN ALDOLASES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of the type I fructose 1,6-bisphosphate aldolase from human | + | The structure of the type I fructose 1,6-bisphosphate aldolase from human muscle has been extended from 3 A to 2 A resolution. The improvement in the resulting electron density map is such that the 20 or so C-terminal residues, known to be associated with activity and isozyme specificity, have been located. The side-chain of the Schiff's base-forming lysine 229 is located towards the centre of an eight-stranded beta-barrel type structure. The C-terminal "tail" extends from the rim of the beta-barrel towards lysine 229, thus forming part of the active site of the enzyme. This structural arrangement appears to explain the difference in activity and specificity of the three tissue-specific human aldolases and helps with our understanding of the type I aldolase reaction mechanism. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ALD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13] Full crystallographic information is available from [http:// | + | 1ALD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALD OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Watson, H | + | [[Category: Watson, H C.]] |
[[Category: lyase (aldehyde)]] | [[Category: lyase (aldehyde)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:45:47 2008'' |
Revision as of 09:45, 21 February 2008
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ACTIVITY AND SPECIFICITY OF HUMAN ALDOLASES
Contents |
Overview
The structure of the type I fructose 1,6-bisphosphate aldolase from human muscle has been extended from 3 A to 2 A resolution. The improvement in the resulting electron density map is such that the 20 or so C-terminal residues, known to be associated with activity and isozyme specificity, have been located. The side-chain of the Schiff's base-forming lysine 229 is located towards the centre of an eight-stranded beta-barrel type structure. The C-terminal "tail" extends from the rim of the beta-barrel towards lysine 229, thus forming part of the active site of the enzyme. This structural arrangement appears to explain the difference in activity and specificity of the three tissue-specific human aldolases and helps with our understanding of the type I aldolase reaction mechanism.
Disease
Known disease associated with this structure: Aldolase A deficiency OMIM:[103850]
About this Structure
1ALD is a Single protein structure of sequence from Homo sapiens. Active as Fructose-bisphosphate aldolase, with EC number 4.1.2.13 Full crystallographic information is available from OCA.
Reference
Activity and specificity of human aldolases., Gamblin SJ, Davies GJ, Grimes JM, Jackson RM, Littlechild JA, Watson HC, J Mol Biol. 1991 Jun 20;219(4):573-6. PMID:2056525
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