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Literature summary extracted from

  • Zheng, Y.; Chen, C.C.; Ko, T.P.; Xiao, X.; Yang, Y.; Huang, C.H.; Qian, G.; Shao, W.; Guo, R.T.
    Crystal structures of S-adenosylhomocysteine hydrolase from the thermophilic bacterium Thermotoga maritima (2015), J. Struct. Biol., 190, 135-142 .
    View publication on PubMed

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.13.2.1 purified recombinant His-tagged enzyme, sitting drop vapor diffusion method, mixing of 10 mg/ml protein in 150 mM NaCl, 25 mM Tris-HCl, pH 7.5, 10 mM DTT, and 2 mM NAD+ with 0.001 ml of reservoir solution containing 4.3 M NaNO3, and 0.1 M NaAc, pH 4.6, and equilibration against 0.3 ml of reservoir solution at room temperature, method optimization, X-ray diffraction structure determination and analysis at 2.04 A resolution. Crystals of tmSAHH in complex with both SAH and NAD+ are obtained by soaking and cocrystallization with resolution at 2.85 A. Molecular replacement using the Rattus norvegicus SAHH structure, PDB ID 1B3R, as search model 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
-
 r
3.13.2.1 S-adenosyl-L-homocysteine + H2O Thermotoga maritima DSM 3109
-
 L-homocysteine + adenosine
-
 r
3.13.2.1 S-adenosyl-L-homocysteine + H2O Thermotoga maritima ATCC 43589
-
 L-homocysteine + adenosine
-
 r
3.13.2.1 S-adenosyl-L-homocysteine + H2O Thermotoga maritima JCM 10099
-
 L-homocysteine + adenosine
-
 r

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)-RIL by nickel affinity chromatography and dialysis 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
-
 r
3.13.2.1 S-adenosyl-L-homocysteine + H2O substrate binding site structure, overview Thermotoga maritima L-homocysteine + adenosine
-
 r
3.13.2.1 S-adenosyl-L-homocysteine + H2O
-
 Thermotoga maritima DSM 3109 L-homocysteine + adenosine
-
 r
3.13.2.1 S-adenosyl-L-homocysteine + H2O substrate binding site structure, overview Thermotoga maritima DSM 3109 L-homocysteine + adenosine
-
 r
3.13.2.1 S-adenosyl-L-homocysteine + H2O
-
 Thermotoga maritima ATCC 43589 L-homocysteine + adenosine
-
 r
3.13.2.1 S-adenosyl-L-homocysteine + H2O substrate binding site structure, overview Thermotoga maritima ATCC 43589 L-homocysteine + adenosine
-
 r
3.13.2.1 S-adenosyl-L-homocysteine + H2O
-
 Thermotoga maritima JCM 10099 L-homocysteine + adenosine
-
 r
3.13.2.1 S-adenosyl-L-homocysteine + H2O substrate binding site structure, overview Thermotoga maritima JCM 10099 L-homocysteine + adenosine
-
 r

Subunits

EC Number Subunits Comment Organism
3.13.2.1 homotetramer each subunit of the tetrameric enzyme is composed of three domains, namely the catalytic domain, the NAD+-binding domain and the C-terminal domain Thermotoga maritima

Synonyms

EC Number Synonyms Comment Organism
3.13.2.1 S-adenosylhomocysteine hydrolase
-
 Thermotoga maritima
3.13.2.1 SAH hydrolase
-
 Thermotoga maritima
3.13.2.1 tmSAHH
-
 Thermotoga maritima

Cofactor

EC Number Cofactor Comment Organism Structure
3.13.2.1 NAD+ NAD+ binding mode, overview. Two cysteine residues in mesophilic enzymes are replaced by serine and threonine in tmSAHH, and the C-terminal domain of tmSAHH lacks the second loop region of mesophilic SAHH, which is important in NAD+ binding, and thus exposes the bound cofactor to the solvent. The difference explains the higher NAD+ requirement of tmSAHH because of the reduced affinity. Binding pocket structure, overview Thermotoga maritima

General Information

EC Number General Information Comment Organism
3.13.2.1 evolution two cysteine residues in mesophilic enzymes are replaced by serine and threonine in tmSAHH, and the C-terminal domain of tmSAHH lacks the second loop region of mesophilic SAHH the feature of missing loop is consistently observed in thermophilic bacterial and archaeal SAHHs. The differences explain the higher NAD+ requirement of tmSAHH because of the reduced affinity and may be related to the thermostability Thermotoga maritima
3.13.2.1 additional information both catalytic domain and NAD+-binding domain show a typical alpha/beta twist structure. The core of the catalytic domain is a seven-stranded parallel beta-sheet in the center, which is surrounded by four and three alpha-helices on the two sides. The beta-sheet in the core of the NAD+-binding domain is composed of five parallel and two antiparallel strands, sandwiched by three and two alpha-helices. Structure determination of the unique C-terminal domain of tmSAHH, overview Thermotoga maritima