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PDBsum entry 4dbc

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protein ligands links
Transferase PDB id
4dbc
Jmol
Contents
Protein chain
396 a.a.
Ligands
SO4 ×4
EDO
3QP
Waters ×447
PDB id:
4dbc
Name: Transferase
Title: Substrate activation in aspartate aminotransferase
Structure: Aspartate aminotransferase. Chain: a. Synonym: aspat, transaminase a. Mutation: yes
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12
Resolution:
1.50Å     R-factor:   0.170     R-free:   0.194
Authors: M.D.Toney,A.J.Fisher,W.R.Griswold
Key ref: W.R.Griswold et al. (2012). Ground-state electronic destabilization via hyperconjugation in aspartate aminotransferase. J Am Chem Soc, 134, 8436-8438. PubMed id: 22551424 DOI: 10.1021/ja302809e
Date:
14-Jan-12     Release date:   05-Dec-12    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00509  (AAT_ECOLI) -  Aspartate aminotransferase
Seq:
Struc:
396 a.a.
396 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.2.6.1.1  - Aspartate transaminase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
L-aspartate
+ 2-oxoglutarate
= oxaloacetate
+ L-glutamate
      Cofactor: Pyridoxal 5'-phosphate
Pyridoxal 5'-phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   2 terms 
  Biological process     biosynthetic process   4 terms 
  Biochemical function     catalytic activity     8 terms  

 

 
    reference    
 
 
DOI no: 10.1021/ja302809e J Am Chem Soc 134:8436-8438 (2012)
PubMed id: 22551424  
 
 
Ground-state electronic destabilization via hyperconjugation in aspartate aminotransferase.
W.R.Griswold, J.N.Castro, A.J.Fisher, M.D.Toney.
 
  ABSTRACT  
 
Binding isotope effects for l-aspartate reacting with the inactive K258A mutant of PLP-dependent aspartate aminotransferase to give a stable external aldimine intermediate are reported. They provide direct evidence for electronic ground-state destabilization via hyperconjugation. The smaller equilibrium isotope effect with deazaPLP-reconstituted K258A indicates that the pyridine nitrogen plays an important role in labilizing the Cα-H bond.