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Literature summary extracted from

  • Brzezinski, K.; Czyrko, J.; Sliwiak, J.; Nalewajko-Sieliwoniuk, E.; Jaskolski, M.; Nocek, B.; Dauter, Z.
    S-adenosyl-L-homocysteine hydrolase from a hyperthermophile (Thermotoga maritima) is expressed in Escherichia coli in inactive form - Biochemical and structural studies (2017), Int. J. Biol. Macromol., 104, 584-596 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.13.2.1 gene sahH, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3) Thermotoga maritima

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.13.2.1 purified recombinant enzyme free or in complex with adenosine, hanging drop vapour diffusion method, mixing of 0.002 ml of 6 mg/ml protein in 100 mM NaCl, and 25 mM Tris-HCl, pH 8.0, with 0.002 ml of reservoir solution containing 20 mM MgCl2 or CaCl2, 0.1 M sodium acetate, pH 4.6 or pH 5.3, and 30% v/v MPD for crystal structure 1 or 2, respectively, with or without addition of adenosine, 18°C, X-ray diffraction structure determination and analysis at 1.75-1.90 A resolution, molecular replacement using the substrate-binding (residues 18-181 and 355-421) and cofactor-binding (182-354) domains of a model of Homo sapiens SAHase (PDB ID 1LI4) as search model Thermotoga maritima

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.13.2.1 additional information
-
 additional information thermodynamics and kinetics, recombinant enzyme Thermotoga maritima

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.13.2.1 S-adenosyl-L-homocysteine + H2O Thermotoga maritima
-
 L-homocysteine + adenosine
-
 ?
3.13.2.1 S-adenosyl-L-homocysteine + H2O Thermotoga maritima DSM 3109
-
 L-homocysteine + adenosine
-
 ?
3.13.2.1 S-adenosyl-L-homocysteine + H2O Thermotoga maritima ATCC 43589
-
 L-homocysteine + adenosine
-
 ?
3.13.2.1 S-adenosyl-L-homocysteine + H2O Thermotoga maritima JCM 10099
-
 L-homocysteine + adenosine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.13.2.1 Thermotoga maritima O51933
-
-
3.13.2.1 Thermotoga maritima ATCC 43589 O51933
-
-
3.13.2.1 Thermotoga maritima DSM 3109 O51933
-
-
3.13.2.1 Thermotoga maritima JCM 10099 O51933
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.13.2.1 recombinant His-tagged enzyme from Escherichia coli strain BL21-CodonPlus(DE3) by nickel affinity chromatography, followed by tag cleavage through TEV protease, dialysis, another step of nickel affinity chromatography, ammonium sulfate fractionation, and ultrafiltration, gel filtration, and again ultrafiltration Thermotoga maritima

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.13.2.1 S-adenosyl-L-homocysteine + H2O
-
 Thermotoga maritima L-homocysteine + adenosine
-
 ?
3.13.2.1 S-adenosyl-L-homocysteine + H2O
-
 Thermotoga maritima DSM 3109 L-homocysteine + adenosine
-
 ?
3.13.2.1 S-adenosyl-L-homocysteine + H2O
-
 Thermotoga maritima ATCC 43589 L-homocysteine + adenosine
-
 ?
3.13.2.1 S-adenosyl-L-homocysteine + H2O
-
 Thermotoga maritima JCM 10099 L-homocysteine + adenosine
-
 ?

Subunits

EC Number Subunits Comment Organism
3.13.2.1 homotetramer 4 * 45000, recombinant enzyme, SDS-PAGE Thermotoga maritima
3.13.2.1 More calorimetric evaluation of heat-induced conformational changes at 85°C and oligomeric state Thermotoga maritima

Synonyms

EC Number Synonyms Comment Organism
3.13.2.1 S-adenosyl-L-homocysteine hydrolase
-
 Thermotoga maritima
3.13.2.1 SAHase
-
 Thermotoga maritima

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.13.2.1 additional information
-
 the enzyme is inactive at room temperature, mechanism of thermal activation, overview. calorimetric evaluation of heat-induced conformational changes (at 85°C) and oligomeric state Thermotoga maritima

Cofactor

EC Number Cofactor Comment Organism Structure
3.13.2.1 NAD+
-
 Thermotoga maritima

General Information

EC Number General Information Comment Organism
3.13.2.1 additional information overall structure of the inactive form of TmSAHase, overview Thermotoga maritima