EC Number | Cloned (Comment) | Organism |
---|---|---|
1.2.1.3 | gene TTC0513, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 Star (DE3) | Thermus thermophilus |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.2.1.3 | purified recombinant enzyme in apoform and in complex with NAD(P)+ and propanal, sitting drop vapor diffusion method, mixing of 20 mg/ml protein in 50 mM Tris-HCl, pH 7.5, 5 mM 2-mercaptoethanol, and 150 mM NaCl, with or without 1 mM NAD(P)+ and 50 mM propanal, with crystallization solution containing 50 mM MOPS, pH 7.5, and 1.2 M ammonium sulfate, 20°C, X-ray diffraction structure determination and analysis | Thermus thermophilus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.2.1.3 | 2.76 | - |
propanal | pH 8.0, 50°C, recombinant wild-type enzyme | Thermus thermophilus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.2.1.3 | Thermus thermophilus | Q72KD3 | - |
- |
1.2.1.3 | Thermus thermophilus ATCC BAA-163 | Q72KD3 | - |
- |
1.2.1.3 | Thermus thermophilus DSM 7039 | Q72KD3 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.2.1.3 | recombinant His-tagged enzyme from Escherichia coli strain BL21 Star (DE3) by nickel affinity chromatography, dialysis, ultrafiltration, and gel filtration. ALDHTt is purified from the caa3-oxidase by cation exchange chromatography and ammonium sulfate precipitation | Thermus thermophilus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.2.1.3 | additional information | 70°C is the best growth temperature of Thermus thermophilus | Thermus thermophilus | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.2.1.3 | hexanal + NAD+ + H2O | - |
Thermus thermophilus | hexanoate + NADH + H+ | - |
? | |
1.2.1.3 | hexanal + NAD+ + H2O | - |
Thermus thermophilus DSM 7039 | hexanoate + NADH + H+ | - |
? | |
1.2.1.3 | hexanal + NAD+ + H2O | - |
Thermus thermophilus ATCC BAA-163 | hexanoate + NADH + H+ | - |
? | |
1.2.1.3 | propanal + NAD+ + H2O | - |
Thermus thermophilus | propionate + NADH + H+ | - |
? | |
1.2.1.3 | propanal + NAD+ + H2O | - |
Thermus thermophilus DSM 7039 | propionate + NADH + H+ | - |
? | |
1.2.1.3 | propanal + NAD+ + H2O | - |
Thermus thermophilus ATCC BAA-163 | propionate + NADH + H+ | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.2.1.3 | More | the quaternary structure of Thermus thermophilus strain HB27 aldehyde dehydrogenase is stabilized by an evolutionary distinct C-terminal arm extension, the enzyme from Thermus thermophilus strain HB8 lacks this extension | Thermus thermophilus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.2.1.3 | ALDHTt | - |
Thermus thermophilus |
1.2.1.3 | More | cf. EC 1.2.1.5 | Thermus thermophilus |
1.2.1.3 | TTC0513 | - |
Thermus thermophilus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.2.1.3 | 50 | - |
assay at | Thermus thermophilus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.2.1.3 | 8 | - |
assay at | Thermus thermophilus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.2.1.3 | NAD+ | - |
Thermus thermophilus | |
1.2.1.3 | NADP+ | binding and catalytic residues conformations in ALDHTt, overview | Thermus thermophilus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.2.1.3 | evolution | enzyme ALDHTt belongs to the ALDH superfamily | Thermus thermophilus |
1.2.1.3 | additional information | enzyme structure analysis and modeling, overview. ALDHTt adopts the ALDH superfamily common structural architecture. The ALDHTt monomer is composed of the three domains common to all ALDHs: (i) The NAD(P)+ binding domain (1-125 + 148-261) comprising a Rossman fold, (ii) the catalytic domain (267-458) and (iii) the oligomerization domain (126-147 + 494-501). (i, ii) are separated by two loops, a short linker loop region containing Glu261 (261-267), required to activate the catalytic cysteine Cys295, and a long inter-domain linker (459-493) harboring the aldehyde anchor loop (464-466). This anchor loop, containing regulatory residues such as the substrate entry channel (SEC) mouth residue and the gating aromatic residue, interacts with the substrate and product. The catalytic and cofactor-binding domains form a central tunnel through the monomer with NAD(P)+ at one side and the classical entrance for substrate on the opposite side. The catalytic residues are deep within the center of the tunnel about 16 A from the cofactor binding site to Glu261 and substrate entry tunnel to the catalytic Cys295. The tunnel is about 5 A in diameter at its widest point | Thermus thermophilus |