EC Number   |
General Information |
Reference |
|---|
   4.1.99.5 | more |
Glu144, one of the iron-coordinating residues, plays a vital role in the catalytic reaction of cADO. The helix, in which Glu144 resides, exhibits two distinct conformations that correlate with the different binding states of the di-iron center in cADO structures. Enzyme structure analysis, comparisons of wild-type and mutant structures, overview. A continuous tube-shaped non-protein electron density, resembling a lipid molecule, is observed close to the di-iron center in all structures but the Y122F structure, a hydrophobic substrate channel in SeADO is described |
-, 749212 |
| 4.1.99.5 | more |
residue L194, at the center of the hydrophobic cavity, might serve as a gateway for substrate entry, but L194 does not play a kinetically significant role in limiting substrate access to the active site. Structure of metal-free cADO, overview |
-, 746597 |
| 4.1.99.5 | more |
residues close to the di-iron center (Tyr39, Gln110, Tyr122), the protein surface (Trp178), and involved in the hydrogen-bonding network (Arg62, Asp143) and the oligopeptide whose conformation changed (Leu/Thr146, Leu148, Asn149 and Tyr/Phe150) in the absence of the diiron center are identified. Comparison of the enzyme from Synechococcus elongates strain PCC 7942 and Synechocystis sp. PCC 6803, the first is more active than the latter against n-hexadecanal. Enzyme structure-function relationship analysis and comparisons, overview |
-, 747409 |
| 4.1.99.5 | more |
solvent isotope effects on alkane formation by cyanobacterial aldehyde deformylating oxygenase and their mechanistic implications, overview |
-, 747074 |
| 4.1.99.5 | more |
the definitive reaffirmation of the oxygenative nature of the reaction implies that the enzyme, initially designated as aldehyde decarbonylase when the C1-derived coproduct is thought to be carbon monoxide rather than formate, should be redesignated as aldehyde-deformylating oxygenase, ADO |
727001 |
| 4.1.99.5 | more |
the enzyme shows a mainly alpha helical architecture, with a ferritin-like four-helix bundle. The latter contains the di-iron centre, coordinated by two histidine residues and four carboxylates from glutamate side chains. Substrates access the active site through a tunnel-like hydrophobic pocket. Active site structure analysis from crystal structure, PDB ID 20C5 |
-, 727312 |
| 4.1.99.5 | more |
the enzyme structure consists of eight a-helices found in ferritin-like di-iron proteins. Residues Tyr21, Ile27, Val28, Phe67, Phe86, Phe87, Phe117, Ala118, Ala121, Tyr122, Try125, and Tyr184 contributing to substrate binding, and Glu32, Glu60, His63, Glu115, Glu144, and His147 participating in iron coordination. OsADO structure resembles ADO structures with active sites containing both metal co-factor and substrate, OsADO active site is fully occupied, helix 5 of OsADO with an iron bound in the active site is a long helix |
746976 |
| 4.1.99.5 | more |
the enzyme structure consists of eight a-helices found in ferritin-like di-iron proteins. Residues Tyr21, Ile27, Val28, Phe67, Phe86, Phe87, Phe117, Ala118, Ala121, Tyr122, Try125, and Tyr184 contributing to substrate binding, and Glu32, Glu60, His63, Glu115, Glu144, and His147 participating in iron coordination. The LiADO structure resembles ADO structures with an empty active site, the LiADO active site is vacant of iron and substrates, helix 5 of LiADO, which lacks iron in the active site, presents two conformations (one long and two short helices), indicating that an equilibrium exists between the two states in solution |
-, 746976 |
| 4.1.99.5 | more |
the synthetic iron(III)-peroxo complex [FeIII(eta2deltaO2)(TMC)]+ (TMC is tetramethylcyclam) causes a similar transformation in the presence of a suitable H atom donor, thus serving as a functional model for cADO, reaction analysis with undecanal with [FeIII(TMC)(delta2deltaO2)]+, detailed overview |
-, 748032 |
| 4.1.99.5 | more |
the very low activity of the enzyme appears to result from inhibition by the ferredoxin reducing system used in the assay and the low solubility of the substrate |
-, 726957 |
