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Literature summary for 3.13.2.1 extracted from

  • Malecki, P.H.; Imiolczyk, B.; Barciszewski, J.; Czyrko-Horczak, J.; Sliwiak, J.; Gawel, M.; Wozniak, K.; Jaskolski, M.; Brzezinski, K.
    Biochemical and structural insights into an unusual, alkali-metal-independent S-adenosyl-L-homocysteine hydrolase from Synechocystis sp. PCC 6803 (2022), Acta Crystallogr. Sect. D, 78, 865-882 .
    View publication on PubMed
Search for more literature for 3.13.2.1

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21 Synechocystis sp. PCC 6803

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapor-diffusion method Synechocystis sp. PCC 6803

Protein Variants

Protein Variants Comment Organism
E352T mutant enzyme is completely inactive Synechocystis sp. PCC 6803
R24E substrate affinity (Km) is not affected by the R24E substitution Synechocystis sp. PCC 6803
R24E/E352T mutant enzyme is completely inactive Synechocystis sp. PCC 6803

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00473
-
 S-adenosyl-L-homocysteine pH 7.5, 20°C, wild-type enzyme, 100 mM K+ Synechocystis sp. PCC 6803
0.00477
-
 S-adenosyl-L-homocysteine pH 7.5, 20°C, mutant enzyme R24E, 100 mM K+ Synechocystis sp. PCC 6803
0.00534
-
 S-adenosyl-L-homocysteine pH 7.5, 20°C, wild-type enzyme, 100 mM Na+ Synechocystis sp. PCC 6803
0.00614
-
 S-adenosyl-L-homocysteine pH 7.5, 20°C, wild-type enzyme, 100 mM Rb+ Synechocystis sp. PCC 6803
0.00682
-
 S-adenosyl-L-homocysteine pH 7.5, 20°C, wild-type enzyme, 100 mM Li+ Synechocystis sp. PCC 6803
0.0073
-
 S-adenosyl-L-homocysteine pH 7.5, 20°C, wild-type enzyme, without monovalent metal ion Synechocystis sp. PCC 6803

Metals/Ions

Metals/Ions Comment Organism Structure
additional information activity and ligand binding of the enzyme are not affected by the presence of any particular alkali ion Synechocystis sp. PCC 6803

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
92000
-
 dimeric enzyme form, gel filtration Synechocystis sp. PCC 6803
184000
-
 tetrameric enzyme form, gel filtration Synechocystis sp. PCC 6803

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-homocysteine + H2O Synechocystis sp. PCC 6803
-
 L-homocysteine + adenosine
-
 ?

Organism

Organism UniProt Comment Textmining
Synechocystis sp. PCC 6803 P74008
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Synechocystis sp. PCC 6803

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-homocysteine + H2O
-
 Synechocystis sp. PCC 6803 L-homocysteine + adenosine
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 46000, SDS-PAGE, the cyanobacterial enzyme is in an equilibrium of two distinct oligomeric states corresponding to its dimeric and tetrameric forms in solution Synechocystis sp. PCC 6803
tetramer 4 * 46000, SDS-PAGE, the cyanobacterial enzyme is in an equilibrium of two distinct oligomeric states corresponding to its dimeric and tetrameric forms in solution Synechocystis sp. PCC 6803

Synonyms

Synonyms Comment Organism
SAHase
-
 Synechocystis sp. PCC 6803

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.011
-
 S-adenosyl-L-homocysteine pH 7.5, 20°C, mutant enzyme R24E, 100 mM K+ Synechocystis sp. PCC 6803
0.175
-
 S-adenosyl-L-homocysteine pH 7.5, 20°C, wild-type enzyme, 100 mM Rb+ Synechocystis sp. PCC 6803
0.178
-
 S-adenosyl-L-homocysteine pH 7.5, 20°C, wild-type enzyme, without monovalent metal ion Synechocystis sp. PCC 6803
0.186
-
 S-adenosyl-L-homocysteine pH 7.5, 20°C, wild-type enzyme, 100 mM K+ Synechocystis sp. PCC 6803
0.186
-
 S-adenosyl-L-homocysteine pH 7.5, 20°C, wild-type enzyme, 100 mM Li+ Synechocystis sp. PCC 6803
0.192
-
 S-adenosyl-L-homocysteine pH 7.5, 20°C, wild-type enzyme, 100 mM Na+ Synechocystis sp. PCC 6803

General Information

General Information Comment Organism
physiological function essential enzyme involved in the regulation of cellular S-adenosyl-L-methionine-dependent methylation reactions Synechocystis sp. PCC 6803

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.2
-
 S-adenosyl-L-homocysteine pH 7.5, 20°C, mutant enzyme R24E, 100 mM K+ Synechocystis sp. PCC 6803
24.3
-
 S-adenosyl-L-homocysteine pH 7.5, 20°C, wild-type enzyme, without monovalent metal ion Synechocystis sp. PCC 6803
27.2
-
 S-adenosyl-L-homocysteine pH 7.5, 20°C, wild-type enzyme, 100 mM Li+ Synechocystis sp. PCC 6803
28.5
-
 S-adenosyl-L-homocysteine pH 7.5, 20°C, wild-type enzyme, 100 mM Rb+ Synechocystis sp. PCC 6803
36
-
 S-adenosyl-L-homocysteine pH 7.5, 20°C, wild-type enzyme, 100 mM Na+ Synechocystis sp. PCC 6803
39.3
-
 S-adenosyl-L-homocysteine pH 7.5, 20°C, wild-type enzyme, 100 mM K+ Synechocystis sp. PCC 6803