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PDBsum entry 1rqx

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
1rqx
Jmol
Contents
Protein chains
331 a.a. *
Ligands
PLP-MLP ×4
Waters ×361
* Residue conservation analysis
PDB id:
1rqx
Name: Hydrolase
Title: Crystal structure of acc deaminase complexed with inhibitor
Structure: 1-aminocyclopropane-1-carboxylate deaminase. Chain: a, b, c, d. Synonym: acc deaminase. Engineered: yes
Source: Pseudomonas sp.. Organism_taxid: 74568. Strain: acp. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Tetramer (from PQS)
Resolution:
2.50Å     R-factor:   0.202     R-free:   0.248
Authors: S.Karthikeyan,Z.Zhao,C.L.Kao,Q.Zhou,Z.Tao,H.Zhang,H.W.Liu
Key ref: S.Karthikeyan et al. (2004). Structural analysis of 1-aminocyclopropane-1-carboxylate deaminase: observation of an aminyl intermediate and identification of Tyr 294 as the active-site nucleophile. Angew Chem Int Ed Engl, 43, 3425-3429. PubMed id: 15221829 DOI: 10.1002/anie.200453353
Date:
07-Dec-03     Release date:   17-Aug-04    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q00740  (1A1D_PSEUD) -  1-aminocyclopropane-1-carboxylate deaminase
Seq:
Struc:
338 a.a.
331 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.5.99.7  - 1-aminocyclopropane-1-carboxylate deaminase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3
1-aminocyclopropane-1-carboxylate
+ H(2)O
= 2-oxobutanoate
+ NH(3)
      Cofactor: Pyridoxal 5'-phosphate
Pyridoxal 5'-phosphate
Bound ligand (Het Group name = PLP) matches with 93.75% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     amine catabolic process   2 terms 
  Biochemical function     hydrolase activity     3 terms  

 

 
    reference    
 
 
DOI no: 10.1002/anie.200453353 Angew Chem Int Ed Engl 43:3425-3429 (2004)
PubMed id: 15221829  
 
 
Structural analysis of 1-aminocyclopropane-1-carboxylate deaminase: observation of an aminyl intermediate and identification of Tyr 294 as the active-site nucleophile.
S.Karthikeyan, Z.Zhao, C.L.Kao, Q.Zhou, Z.Tao, H.Zhang, H.W.Liu.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
18825405 B.Todorovic, and B.R.Glick (2008).
The interconversion of ACC deaminase and D: -cysteine desulfhydrase by directed mutagenesis.
  Planta, 229, 193-205.  
17665234 M.Saleem, M.Arshad, S.Hussain, and A.S.Bhatti (2007).
Perspective of plant growth promoting rhizobacteria (PGPR) containing ACC deaminase in stress agriculture.
  J Ind Microbiol Biotechnol, 34, 635-648.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.