Difference between revisions of "Aldo-keto reductase family 1 member B1"

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(Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|AR, AKR1B1|[https://www.uniprot.org/uniprot/P15121 P15121]|Homo sapiens|Cys299|[http://pfam.xfam.org/family/PF0...")
 
(Cys Function & Property)
 
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===Cys Function & Property===
 
===Cys Function & Property===
Cys299 is quite clost to the active sites of AKR1B1. <br/>
+
Cys299 is close to the active sites of AKR1B1 in space, include Trp111, Gln49. <br/>
  
 
* Hydrophobic property:
 
* Hydrophobic property:

Latest revision as of 03:08, 22 August 2019

Basic Information
Short Name AR, AKR1B1
UNP ID P15121
Organism Homo sapiens
Cys Site Cys299
Family/Domain Aldo/keto reductase family
Known Ligand Ligand list
Function Type Metabolic enzyme

Summary

Protein Function

Aldose reductase is a member of the aldo-keto reductase (AKR) superfamily (AKR1B1). It catalyzes the NADPH-dependent reduction of a broad spectrum of substrates that range from simple aromatic aldehydes and steroid carbonyls to aldo-keto sugars. The wide substrate specificity of AR suggests that the enzyme may be involved in detoxification of endogenous and xenobiotic aldehydes. (PMID: 18223294)

Cys Function & Property

Cys299 is close to the active sites of AKR1B1 in space, include Trp111, Gln49.

  • Hydrophobic property:
582-hydro.png
  • SASA:
Cys299: 10.044 A^2

Protein Sequence

MASRLLLNNG AKMPILGLGT WKSPPGQVTE AVKVAIDVGY RHIDCAHVYQ
NENEVGVAIQ EKLREQVVKR EELFIVSKLW CTYHEKGLVK GACQKTLSDL
KLDYLDLYLI HWPTGFKPGK EFFPLDESGN VVPSDTNILD TWAAMEELVD
EGLVKAIGIS NFNHLQVEMI LNKPGLKYKP AVNQIECHPY LTQEKLIQYC
QSKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKAIAAK HNKTTAQVLI
RFPMQRNLVV IPKSVTPERI AENFKVFDFE LSSQDMTTLL SYNRNWRVCA
LLSCTSHKDY PFHEEF

Structural Information

  • Known structure with covalent ligand:
Unknown
  • Protein structure:
582.png

Related Pathway

Experimental Evidence

Cys-directed Mutation

Reference

  1. Kaiserova K, Tang X L, Srivastava S, et al. Role of nitric oxide in regulating aldose reductase activation in the ischemic heart[J]. Journal of Biological Chemistry, 2008, 283(14): 9101-9112. 18223294