Literature summary for 1.2.1.3 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 .

Cloned(Commentary)

Cloned (Comment)	Organism
gene TTC0513, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 Star (DE3)	Thermus thermophilus

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
2.76	-	propanal	pH 8.0, 50°C, recombinant wild-type enzyme	Thermus thermophilus

Organism

Organism	UniProt	Comment	Textmining
Thermus thermophilus	Q72KD3	-	-
Thermus thermophilus ATCC BAA-163	Q72KD3	-	-
Thermus thermophilus DSM 7039	Q72KD3	-	-

Purification (Commentary)

Purification (Comment)	Organism
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

Source Tissue	Comment	Organism	Textmining
additional information	70°C is the best growth temperature of Thermus thermophilus	Thermus thermophilus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
hexanal + NAD+ + H2O	-	Thermus thermophilus	hexanoate + NADH + H+	-	?
hexanal + NAD+ + H2O	-	Thermus thermophilus DSM 7039	hexanoate + NADH + H+	-	?
hexanal + NAD+ + H2O	-	Thermus thermophilus ATCC BAA-163	hexanoate + NADH + H+	-	?
propanal + NAD+ + H2O	-	Thermus thermophilus	propionate + NADH + H+	-	?
propanal + NAD+ + H2O	-	Thermus thermophilus DSM 7039	propionate + NADH + H+	-	?
propanal + NAD+ + H2O	-	Thermus thermophilus ATCC BAA-163	propionate + NADH + H+	-	?

Subunits

Subunits	Comment	Organism
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

Synonyms	Comment	Organism
ALDHTt	-	Thermus thermophilus
More	cf. EC 1.2.1.5	Thermus thermophilus
TTC0513	-	Thermus thermophilus

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Thermus thermophilus
NADP+	binding and catalytic residues conformations in ALDHTt, overview	Thermus thermophilus

General Information

General Information	Comment	Organism
evolution	enzyme ALDHTt belongs to the ALDH superfamily	Thermus thermophilus
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