4.1.99.5: aldehyde oxygenase (deformylating)

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For detailed information about aldehyde oxygenase (deformylating), go to the full flat file.

Word Map on EC 4.1.99.5

4.1.99.5

biofuels

decarbonylation

acyl-acyl

punctiforme

elongatus

octadecanal

di-iron

drop-in

cados

heptadecane

ferritin-like

prochlorococcus

diferric

photodecarboxylase

petroleum-derived

biofuel production

Reaction

+ 2 NADPH + 2 H+ =

+ 2 NADP⁺

Synonyms

ADO, aldehyde decarbonylase, aldehyde deformylase, aldehyde deformylating oxygenase, aldehyde-deformylating oxygenase, CAD, cADO, cADO-1593, cyanobacterial ADO, cyanobacterial aldehyde decarbonylase, cyanobacterial aldehyde deformylating oxygenase, cyanobacterial aldehyde-deformylating oxygenase, decarbonylase, erial aldehyde-deformylating oxygenase, LiADO, More, Npun_R1711, OsADO, PMT1231, PMT_1231, RS9917_09941, SeADO, sll0208, Synpcc7942_1593

ECTree

4 Lyases

4.1 Carbon-carbon lyases

4.1.99 Other carbon-carbon lyases

4.1.99.5 aldehyde oxygenase (deformylating)

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Results	in table
8	Activating Compound
2057	AA Sequence
5	Application
1	CAS Registry Number
25	Cloned(Commentary)
33	Cofactor
4	Crystallization (Commentary)
57	General Information
2	General Stability
33	Inhibitors
17	kcat/KM [mM/s]
23	KM Value [mM]
11	Localization
18	Metals/Ions
6	Molecular Weight [Da]
46	Natural Substrates/ Products (Substrates)
2	Organic Solvent Stability
98	Organism
3	Oxidation Stability
5	Pathway
29	PDB ID
20	pH Optimum
3	pH Range
87	Protein Variants
14	Purification (Commentary)
21	Reaction
1	Reaction Type
56	Reference
4	Source Tissue
2	Specific Activity [micromol/min/mg]
192	Substrates and Products (Substrate)
15	Subunits
121	Synonyms
1	Systematic Name
24	Temperature Optimum [°C]
8	Temperature Stability [°C]
42	Turnover Number [1/s]

Crystallization

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Crystallization on EC 4.1.99.5 - aldehyde oxygenase (deformylating)

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crystal structure determination and analysis

2 entries

purified recombinant wild-type and mutant L194A in complex with 11-(2-(2-ethoxyethoxy)ethoxy)undecanal, trans-2-nonylcyclopropane-1-carboxylic acid, or stearate, X-ray diffraction structure determination and analysis at 1.60-2.21 A resolution. It appears that the fatty acids are necessary for crystallization. Attempts to crystallize the enzyme in fully metalated form by including Fe2+ or Zn2+ ions in the crystallization buffer together with 11-(2-(2-ethoxyethoxy)ethoxy)undecanal are unsuccessful

Prochlorococcus marinus

Q7V6D4

746597

purified recombinant enzyme in both its iron-free and iron-bound forms or with bound substrate, and of mutants Y122F and F86Y/F87Y, sitting drop vapor diffusion method, from reservoir solution of 0.2 mol/l Mg2+, 0.1 mol/l Tris, pH 8.5, 30% w/v PEG 4000, for the iron-bound crystals, 4 mM ferrous ammonium sulfate is added to SeADO protein solutions right before crystallization, and for the substrate-bound enzyme, 0.2mol/l L-proline, 0.1mol/l HEPES, pH 7.1, 25% w/v PEG 1500 is used, 18°C, X-ray diffraction structure determination and analysis at 1.71-2.9 A resolution

Synechococcus elongatus PCC 7942 = FACHB-805

Q54764

749212