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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.B21
-
 Pyrococcus horikoshii
2.5.1.B21 expression in Escherichia coli BL21(DE3) Salinispora arenicola

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.5.1.B21 recombinant enzyme, sitting-drop vapour diffusion technique Pyrococcus horikoshii

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.B21 D72A complete loss of activity Salinispora arenicola
2.5.1.B21 H130A 25% of wild-type activity Salinispora arenicola
2.5.1.B21 H130Y 5% of wild-type activity Salinispora arenicola
2.5.1.B21 R79A almost inactive protein Salinispora arenicola

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.B21 0.001
-
 S-adenosyl-L-methionine pH 7.9, 37°C, wild-type enzyme Salinispora arenicola
2.5.1.B21 0.0014
-
 S-adenosyl-L-methionine pH 7.9, 37°C, mutant enzyme H130A Salinispora arenicola
2.5.1.B21 0.0017
-
 S-adenosyl-L-methionine pH 7.9, 37°C, mutant enzyme H130Y Salinispora arenicola

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.B21 Pyrococcus horikoshii O58212
-
-
2.5.1.B21 Salinispora arenicola
-
-
-
2.5.1.94 Salinispora tropica
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.B21
-
 Pyrococcus horikoshii
2.5.1.B21
-
 Salinispora arenicola

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.B21 S-adenosyl-L-methionine + H2O
-
 Salinispora arenicola adenosine + L-methionine + H+
-
 ?
2.5.1.B21 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+
-
 ?
2.5.1.94 S-adenosyl-L-methionine + chloride chlorinase catalyzes chloride ion SN2 substitution at the C5' of S-adenosyl-L-methionine to generate 5'-deoxy-5'-chloroadenosine Salinispora tropica 5'-deoxy-5'-chloroadenosine + L-methionine
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.5.1.B21 SAM hydroxide adenosyltransferase
-
 Salinispora arenicola
2.5.1.94 chlorinase
-
 Salinispora tropica

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.5.1.B21 37
-
 assay at Salinispora arenicola

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.5.1.B21 0.0007
-
 S-adenosyl-L-methionine pH 7.9, 37°C, mutant enzyme H130Y Salinispora arenicola
2.5.1.B21 0.0027
-
 S-adenosyl-L-methionine pH 7.9, 37°C, mutant enzyme H130A Salinispora arenicola
2.5.1.B21 0.0075
-
 S-adenosyl-L-methionine pH 7.9, 37°C, wild-type enzyme Salinispora arenicola

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.B21 7.9
-
 assay at Salinispora arenicola

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.5.1.B21 0.41
-
 S-adenosyl-L-methionine pH 7.9, 37°C, mutant enzyme H130Y Salinispora arenicola
2.5.1.B21 1.9
-
 S-adenosyl-L-methionine pH 7.9, 37°C, mutant enzyme H130A Salinispora arenicola
2.5.1.B21 7.5
-
 S-adenosyl-L-methionine pH 7.9, 37°C, wild-type enzyme Salinispora arenicola