_EC 3.5.99.7 1-aminocyclopropane-1-carboxylate deaminase. 12 PDB entries  
EC 3.-.-.- Hydrolases. [21,295 PDB entries]
EC 3.5.-.- Acting on carbon-nitrogen bonds, other than peptide bonds. [1,690 PDB entries]
EC 3.5.99.- In other compounds. [42 PDB entries]
EC 3.5.99.7 1-aminocyclopropane-1-carboxylate deaminase. [12 PDB entries]    
1f2d

Reaction: 1-aminocyclopropane-1-carboxylate + H(2)O = 2-oxobutanoate + NH(3).
 


1-aminocyclopropane-1-carboxylate
+ H(2)O
=
2-oxobutanoate
+ NH(3)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Other name(s): 1-aminocyclopropane carboxylic acid deaminase. 1-aminocyclopropane-1-carboxylate endolyase (deaminating). Acc deaminase.
Cofactor(s): Pyridoxal 5'-phosphate.
 

Pyridoxal 5'-phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.
Comments: The enzyme, found in certain soil bacteria and fungi, catalyzes the ring opening of 1-aminocyclopropane-1-carboxylate, the immediate precursor to ethylene, an important plant hormone that regulates fruit ripening and other processes. The enzyme releases an unstable enamine product that tautomerizes to an imine form, which undergoes spontaneous hydrolytic deamination. The enzyme has been used to make fruit ripening dependent on externally added ethylene, as it removes the substrate for endogenous ethylene formation. Formerly Ec 4.1.99.4.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 12 PDB entries in enzyme class E.C.3.5.99.7

  PDB code Protein
1f2d
1-aminocyclopropane-1-carboxylate deaminase
Source: Williopsis saturnus. Organism_taxid: 4906. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (341 residues) CATH domains: 3.40.50.1100 3.40.50.1100
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1j0a
Crystal structure analysis of the acc deaminase homologue
Source: Pyrococcus horikoshii. Organism_taxid: 70601. Strain: ot3. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B, C (325 residues) CATH domains: 3.40.50.1100 3.40.50.1100
Bound ligands:   Het Group IPA is 57.14% similar to enzyme product 2-oxobutanoate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1j0b
Crystal structure analysis of the acc deaminase homologue co with inhibitor
Source: Pyrococcus horikoshii. Organism_taxid: 70601. Strain: ot3. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X (325 residues) CATH domains: 3.40.50.1100 3.40.50.1100
Bound ligand:   Het Group 5PA is 65.22% similar to enzyme cofactor pyridoxal
1j0c
Acc deaminase mutated to catalytic residue
Source: Williopsis saturnus. Organism_taxid: 4906. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B, C, D (341 residues) CATH domains: 3.40.50.1100 3.40.50.1100
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1j0d
Acc deaminase mutant complexed with acc
Source: Williopsis saturnus. Organism_taxid: 4906. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B, C, D (341 residues) CATH domains: 3.40.50.1100 3.40.50.1100
Bound ligand:   Het Group 5PA is 65.00% similar to enzyme cofactor pyridoxal 5'-phosphate
1j0e
Acc deaminase mutant reacton intermediate
Source: Williopsis saturnus. Organism_taxid: 4906. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B, C, D (341 residues) CATH domains: 3.40.50.1100 3.40.50.1100
Bound ligands:   Het Group 1AC corresponds to enzyme reactant 1-aminocyclopropane-1-carboxylate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1rqx
Crystal structure of acc deaminase complexed with inhibitor
Source: Pseudomonas sp.. Organism_taxid: 74568. Strain: acp. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (331 residues) CATH domains: 3.40.50.1100 3.40.50.1100
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1tyz
Crystal structure of 1-aminocyclopropane-1-carboyxlate deami pseudomonas
Source: Pseudomonas sp.. Organism_taxid: 74568. Strain: acp. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (331 residues) CATH domains: 3.40.50.1100 3.40.50.1100
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1tz2
Crystal structure of 1-aminocyclopropane-1-carboyxlate deami complexed with acc
Source: Pseudomonas sp.. Organism_taxid: 74568. Strain: acp. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (331 residues) CATH domains: 3.40.50.1100 3.40.50.1100
Bound ligands:   Het Group 1AC corresponds to enzyme reactant 1-aminocyclopropane-1-carboxylate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1tzj
Crystal structure of 1-aminocyclopropane-1-carboxylate deami complexed with d-vinyl glycine
Source: Pseudomonas sp.. Organism_taxid: 74568. Strain: acp. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (331 residues) CATH domains: 3.40.50.1100 3.40.50.1100
Bound ligands:   Het Group A3B corresponds to enzyme reactant 1-aminocyclopropane-1-carboxylate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1tzk
Crystal structure of 1-aminocyclopropane-1-carboxylate-deami complexed with alpha-keto-butyrate
Source: Pseudomonas sp.. Organism_taxid: 74568. Strain: acp. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (331 residues) CATH domains: 3.40.50.1100 3.40.50.1100
Bound ligands:   Het Group 2KT corresponds to enzyme product 2-oxobutanoate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1tzm
Crystal structure of acc deaminase complexed with substrate chloro-d-alanine
Source: Pseudomonas sp.. Organism_taxid: 74568. Strain: acp. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (331 residues) CATH domains: 3.40.50.1100 3.40.50.1100
Bound ligands:   Het Group C2N is 75.00% similar to enzyme reactant 1-aminocyclopropane-1-carboxylate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal