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Literature summary extracted from

  • Hayes, K.; Noor, M.; Djeghader, A.; Armshaw, P.; Pembroke, T.; Tofail, S.; Soulimane, T.
    The quaternary structure of Thermus thermophilus aldehyde dehydrogenase is stabilized by an evolutionary distinct C-terminal arm extension (2018), Sci. Rep., 8, 13327 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

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

Crystallization (Commentary)

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

KM Value [mM]

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

Organism

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
-
-

Purification (Commentary)

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

Source Tissue

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
-

Substrates and Products (Substrate)

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+
-
 ?

Subunits

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

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.1.3 50
-
 assay at Thermus thermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.3 8
-
 assay at Thermus thermophilus

Cofactor

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

General Information

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