PDBsum entry 1m7y

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Lyase PDB id
Protein chain
424 a.a. *
Waters ×332
* Residue conservation analysis
PDB id:
Name: Lyase
Title: Crystal structure of apple acc synthase in complex with l- aminoethoxyvinylglycine
Structure: 1-aminocyclopropane-1-carboxylate synthase. Chain: a. Fragment: residues 1-435. Synonym: acc synthase. Engineered: yes
Source: Malus x domestica. Organism_taxid: 3750. Tissue: fruit cortical. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PDB file)
1.60Å     R-factor:   0.205     R-free:   0.219
Authors: G.Capitani,D.Mccarthy,H.Gut,M.G.Gruetter,J.F.Kirsch
Key ref:
G.Capitani et al. (2002). Apple 1-aminocyclopropane-1-carboxylate synthase in complex with the inhibitor L-aminoethoxyvinylglycine. Evidence for a ketimine intermediate. J Biol Chem, 277, 49735-49742. PubMed id: 12228256 DOI: 10.1074/jbc.M208427200
23-Jul-02     Release date:   23-Dec-02    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P37821  (1A1C_MALDO) -  1-aminocyclopropane-1-carboxylate synthase
473 a.a.
424 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     biosynthetic process   4 terms 
  Biochemical function     catalytic activity     5 terms  


DOI no: 10.1074/jbc.M208427200 J Biol Chem 277:49735-49742 (2002)
PubMed id: 12228256  
Apple 1-aminocyclopropane-1-carboxylate synthase in complex with the inhibitor L-aminoethoxyvinylglycine. Evidence for a ketimine intermediate.
G.Capitani, D.L.McCarthy, H.Gut, M.G.Grütter, J.F.Kirsch.
The 1.6-A crystal structure of the covalent ketimine complex of apple 1-aminocyclopropane-1-carboxylate (ACC) synthase with the potent inhibitor l-aminoethoxyvinylglycine (AVG) is described. ACC synthase catalyzes the committed step in the biosynthesis of ethylene, a plant hormone that is responsible for the initiation of fruit ripening and for regulating many other developmental processes. AVG is widely used in plant physiology studies to inhibit the activity of ACC synthase. The structural assignment is supported by the fact that the complex absorbs maximally at 341 nm. These results are not in accord with the recently reported crystal structure of the tomato ACC synthase AVG complex, which claims that the inhibitor only associates noncovalently. The rate constant for the association of AVG with apple ACC synthase was determined by stopped-flow spectrophotometry (2.1 x 10(5) m(-1) s(-1)) and by the rate of loss of enzyme activity (1.1 x 10(5) m(-1) s(-1)). The dissociation rate constant determined by activity recovery is 2.4 x 10(-6) s(-1). Thus, the calculated K(d) value is 10-20 pm.
  Selected figure(s)  
Figure 6.
Fig. 6. A, superposition of the active sites of unliganded (sea green) and AVG-bound (yellow) ACC synthase. Only selected residues are shown. B, the active sites of AVG-bound ACC synthase (gray) and cystathionine -lyase (sea green). C, the C traces of unliganded (yellow) and AVG-bound (blue) ACC synthase. This illustration was prepared with DINO.
Figure 7.
Fig. 7. LIGPLOT (13) representation of the hydrogen bonding between ACC synthase and the AVG·PLP adduct.
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (2002, 277, 49735-49742) copyright 2002.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20689184 S.R.Choudhury, S.K.Singh, S.Roy, and D.N.Sengupta (2010).
An insight into the sequential, structural and phylogenetic properties of banana 1-aminocyclopropane-1-carboxylate synthase 1 and study of its interaction with pyridoxal-5'-phosphate and aminoethoxyvinylglycine.
  J Biosci, 35, 281-294.  
19132085 A.Thomann, E.Lechner, M.Hansen, E.Dumbliauskas, Y.Parmentier, J.Kieber, B.Scheres, and P.Genschik (2009).
Arabidopsis CULLIN3 genes regulate primary root growth and patterning by ethylene-dependent and -independent mechanisms.
  PLoS Genet, 5, e1000328.  
15610350 A.Danon, O.Miersch, G.Felix, R.G.Camp, and K.Apel (2005).
Concurrent activation of cell death-regulating signaling pathways by singlet oxygen in Arabidopsis thaliana.
  Plant J, 41, 68-80.  
15189147 A.C.Eliot, and J.F.Kirsch (2004).
Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations.
  Annu Rev Biochem, 73, 383-415.  
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