2c91

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Revision as of 21:03, 29 October 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="2c91" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c91, resolution 2.30Å" /> '''MOUSE SUCCINIC SEMI...)
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File:2c91.gif


2c91, resolution 2.30Å

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MOUSE SUCCINIC SEMIALDEHYDE REDUCTASE, AKR7A5

OverviewOverview

The aldo-keto reductases make up a superfamily of enzymes which can reduce, a variety of aldehydes and ketones to their corresponding alcohols. Within, each family are distinct preferences for certain substrates, presumably, reflecting their role within the cell. The original member of the AKR7A, subfamily was purified from liver as an aflatoxin dialdehyde reductase, AKR7A1. However, recent additions to the family have revealed that even, closely related enzymes have clear substrate preferences with AKR7A2, AKR7A4, and AKR7A5 showing much higher affinities for succinic, semialdehyde (SSA) than does AKR7A1. To investigate the structural basis, of this specificity, the crystal structure of mouse AKR7A5 has been, determined to better than 2.5 A resolution. The structure is of the, ternary ... [(full description)]

About this StructureAbout this Structure

2C91 is a [Single protein] structure of sequence from [Mus musculus] with PO4, NAP, TLA, MES and GOL as [ligands]. Full crystallographic information is available from [OCA].

ReferenceReference

Crystal structure of mouse succinic semialdehyde reductase AKR7A5: structural basis for substrate specificity., Zhu X, Lapthorn AJ, Ellis EM, Biochemistry. 2006 Feb 14;45(6):1562-70. PMID:16460003

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