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Literature summary extracted from

  • Wang, Y.; Kavran, J.M.; Chen, Z.; Karukurichi, K.R.; Leahy, D.J.; Cole, P.A.
    Regulation of S-adenosylhomocysteine hydrolase by lysine acetylation (2014), J. Biol. Chem., 289, 31361-31372.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.13.2.1 expressed in Escherichia coli BL21(DE3) cells Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.13.2.1 hanging drop vapor diffusion method, using 200 mM sodium formate, 5-20% (w/v) PEG 3350, and 100 mM BisTris, pH 6.0-6.5 Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.13.2.1 D293A the mutant shows reduced catalytic efficiency with S-adenosyl-L-homocysteine compared to the wild type enzyme and no reaction with L-homocysteine Homo sapiens
3.13.2.1 D422K inactive Homo sapiens
3.13.2.1 N27K the mutant shows reduced catalytic efficiency with S-adenosyl-L-homocysteine compared to the wild type enzyme and no reaction with L-homocysteine Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.13.2.1 0.0139
-
 S-adenosyl-L-homocysteine recombinant wild type enzyme, at pH 7.2 and 37°C Homo sapiens
3.13.2.1 0.0231
-
 S-adenosyl-L-homocysteine mutant enzyme N27K, at pH 7.2 and 37°C Homo sapiens
3.13.2.1 0.0334
-
 S-adenosyl-L-homocysteine mutant enzyme D293A, at pH 7.2 and 37°C Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.13.2.1 48000
-
 4 * 48000, SDS-PAGE Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.13.2.1 L-homocysteine + adenosine + H2O Homo sapiens
-
 S-adenosyl-L-homocysteine
-
 r
3.13.2.1 S-adenosyl-L-homocysteine + H2O Homo sapiens
-
 L-homocysteine + adenosine
-
 r

Organism

EC Number Organism UniProt Comment Textmining
3.13.2.1 Homo sapiens P23526
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.13.2.1 acetylation Lys401 and Lys408 acetylation of the enzyme changes hydrogen bonding patterns in its NAD+ binding regions and reduces its catalytic activity Homo sapiens

Purification (Commentary)

EC Number Purification (Comment) Organism
3.13.2.1 chitin bead chromatography and Superdex 200 gel filtration Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.13.2.1 L-homocysteine + adenosine + H2O
-
 Homo sapiens S-adenosyl-L-homocysteine
-
 r
3.13.2.1 S-adenosyl-L-homocysteine + H2O
-
 Homo sapiens L-homocysteine + adenosine
-
 r

Subunits

EC Number Subunits Comment Organism
3.13.2.1 homotetramer 4 * 48000, SDS-PAGE Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.13.2.1 S-adenosylhomocysteine hydrolase
-
 Homo sapiens
3.13.2.1 SAHH
-
 Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.13.2.1 0.4
-
 S-adenosyl-L-homocysteine mutant enzyme N27K, at pH 7.2 and 37°C Homo sapiens
3.13.2.1 0.56
-
 S-adenosyl-L-homocysteine mutant enzyme D293A, at pH 7.2 and 37°C Homo sapiens
3.13.2.1 0.79
-
 S-adenosyl-L-homocysteine recombinant wild type enzyme, at pH 7.2 and 37°C Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
3.13.2.1 NAD+
-
 Homo sapiens

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.13.2.1 17
-
 S-adenosyl-L-homocysteine mutant enzyme D293A, at pH 7.2 and 37°C Homo sapiens
3.13.2.1 17
-
 S-adenosyl-L-homocysteine mutant enzyme N27K, at pH 7.2 and 37°C Homo sapiens
3.13.2.1 57
-
 S-adenosyl-L-homocysteine recombinant wild type enzyme, at pH 7.2 and 37°C Homo sapiens
3.13.2.1 2000
-
 L-homocysteine recombinant wild type enzyme, at pH 7.2 and 37°C Homo sapiens