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2alr

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Revision as of 04:59, 13 February 2020

ALDEHYDE REDUCTASE

Structural highlights

2alr is a 1 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1alr. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:	Alcohol dehydrogenase (NADP(+)), with EC number 1.1.1.2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[AK1A1_HUMAN] Catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. Catalyzes the reduction of mevaldate to mevalonic acid and of glyceraldehyde to glycerol. Has broad substrate specificity. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid. Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs, including the anthracyclines doxorubicin (DOX) and daunorubicin (DAUN).^[1] ^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The crystal structures of porcine and human aldehyde reductase, an enzyme implicated in complications of diabetes, have been determined by X-ray diffraction methods. The crystallographic R factor for the refined porcine aldehyde reductase model is 0.19 at 2.8 A resolution. There are two molecules in the asymmetric unit related by a local non-crystallographic twofold axis. The human aldehyde reductase model has been refined to an R factor of 0.21 at 2.48 A resolution. The amino-acid sequence of porcine aldehyde reductase revealed a remarkable homology with human aldehyde reductase. The coenzyme-binding site residues are conserved and adopt similar conformations in human and porcine aldehyde reductase apo-enzymes. The tertiary structures of aldhyde reductase and aldose reductase are similar and consist of a beta/alpha-barrel, with the coenzyme-binding site located at the carboxy-terminus end of the strands of the barrel. The crystal structure of porcine and human aldehyde reductase should allow in vitro mutagenesis to elucidate the mechanism of action for this enzyme and facilitate the effective design of specific inhibitors.

Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications.,El-Kabbani O, Green NC, Lin G, Carson M, Narayana SV, Moore KM, Flynn TG, DeLucas LJ Acta Crystallogr D Biol Crystallogr. 1994 Nov 1;50(Pt 6):859-68. PMID:15299353^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ O'connor T, Ireland LS, Harrison DJ, Hayes JD. Major differences exist in the function and tissue-specific expression of human aflatoxin B1 aldehyde reductase and the principal human aldo-keto reductase AKR1 family members. Biochem J. 1999 Oct 15;343 Pt 2:487-504. PMID:10510318
↑ Palackal NT, Burczynski ME, Harvey RG, Penning TM. Metabolic activation of polycyclic aromatic hydrocarbon trans-dihydrodiols by ubiquitously expressed aldehyde reductase (AKR1A1). Chem Biol Interact. 2001 Jan 30;130-132(1-3):815-24. PMID:11306097
↑ Bains OS, Takahashi RH, Pfeifer TA, Grigliatti TA, Reid RE, Riggs KW. Two allelic variants of aldo-keto reductase 1A1 exhibit reduced in vitro metabolism of daunorubicin. Drug Metab Dispos. 2008 May;36(5):904-10. doi: 10.1124/dmd.107.018895. Epub 2008 , Feb 14. PMID:18276838 doi:http://dx.doi.org/10.1124/dmd.107.018895
↑ El-Kabbani O, Green NC, Lin G, Carson M, Narayana SV, Moore KM, Flynn TG, DeLucas LJ. Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications. Acta Crystallogr D Biol Crystallogr. 1994 Nov 1;50(Pt 6):859-68. PMID:15299353 doi:10.1107/S0907444994005275

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2alr"

Categories: Homo sapiens | Large Structures | El-Kabbani, O | Oxidoreductase | Tim-barrel

@@ Line 1: / Line 1: @@
 ==ALDEHYDE REDUCTASE==
-<StructureSection load='2alr' size='340' side='right' caption='[[2alr]], [[Resolution|resolution]] 2.48&Aring;' scene=''>
+<StructureSection load='2alr' size='340' side='right'caption='[[2alr]], [[Resolution|resolution]] 2.48&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2alr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1alr 1alr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ALR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ALR FirstGlance]. <br>
@@ Line 30: / Line 30: @@
 ==See Also==
-*[[Aldose Reductase|Aldose Reductase]]
+*[[Aldose reductase 3D structures|Aldose reductase 3D structures]]
 == References ==
 <references/>
@@ Line 36: / Line 36: @@
 </StructureSection>
 [[Category: Homo sapiens]]
+[[Category: Large Structures]]
 [[Category: El-Kabbani, O]]
 [[Category: Oxidoreductase]]
 [[Category: Tim-barrel]]

2alr

From Proteopedia

Revision as of 04:59, 13 February 2020

ALDEHYDE REDUCTASE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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