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Literature summary for 2.5.1.B21 extracted from

  • Deng, H.; McMahon, S.A.; Eustaquio, A.S.; Moore, B.S.; Naismith, J.H.; O'Hagan, D.
    Mechanistic insights into water activation in SAM hydroxide adenosyltransferase (duf-62) (2009), Chembiochem, 10, 2455-2459.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.5.1.B21

Cloned(Commentary)

Cloned (Comment) Organism
-
 Pyrococcus horikoshii
expression in Escherichia coli BL21(DE3) Salinispora arenicola

Crystallization (Commentary)

Crystallization (Comment) Organism
recombinant enzyme, sitting-drop vapour diffusion technique Pyrococcus horikoshii

Protein Variants

Protein Variants Comment Organism
D72A complete loss of activity Salinispora arenicola
H130A 25% of wild-type activity Salinispora arenicola
H130Y 5% of wild-type activity Salinispora arenicola
R79A almost inactive protein Salinispora arenicola

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.001
-
 S-adenosyl-L-methionine pH 7.9, 37°C, wild-type enzyme Salinispora arenicola
0.0014
-
 S-adenosyl-L-methionine pH 7.9, 37°C, mutant enzyme H130A Salinispora arenicola
0.0017
-
 S-adenosyl-L-methionine pH 7.9, 37°C, mutant enzyme H130Y Salinispora arenicola

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii O58212
-
-
Salinispora arenicola
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pyrococcus horikoshii
-
 Salinispora arenicola

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + H2O
-
 Salinispora arenicola adenosine + L-methionine + H+
-
 ?
S-adenosyl-L-methionine + H2O the amino acid Asp-Arg-His triad and particularly the Asp-Arg ion pair appears to play an important role in holding the water for nucleophilic attack as S-adenosyl-L-methionine binds and becomes proximate Pyrococcus horikoshii adenosine + L-methionine + H+
-
 ?

Synonyms

Synonyms Comment Organism
SAM hydroxide adenosyltransferase
-
 Salinispora arenicola

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Salinispora arenicola

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0007
-
 S-adenosyl-L-methionine pH 7.9, 37°C, mutant enzyme H130Y Salinispora arenicola
0.0027
-
 S-adenosyl-L-methionine pH 7.9, 37°C, mutant enzyme H130A Salinispora arenicola
0.0075
-
 S-adenosyl-L-methionine pH 7.9, 37°C, wild-type enzyme Salinispora arenicola

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.9
-
 assay at Salinispora arenicola

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.41
-
 S-adenosyl-L-methionine pH 7.9, 37°C, mutant enzyme H130Y Salinispora arenicola
1.9
-
 S-adenosyl-L-methionine pH 7.9, 37°C, mutant enzyme H130A Salinispora arenicola
7.5
-
 S-adenosyl-L-methionine pH 7.9, 37°C, wild-type enzyme Salinispora arenicola