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Literature summary for 1.2.1.75 extracted from

  • Demmer, U.; Warkentin, E.; Srivastava, A.; Kockelkorn, D.; Pötter, M.; Marx, A.; Fuchs, G.; Ermler, U.
    Structural basis for a bispecific NADP+ and CoA binding site in an archaeal malonyl-coenzyme A reductase (2013), J. Biol. Chem., 288, 6363-6370.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.2.1.75

Application

Application Comment Organism
biotechnology the crystallographic data indicate how to construct a bispecific cofactor binding site and to engineer a malonyl-CoA into methylmalonyl-CoA reductase for polyester building block production Sulfurisphaera tokodaii
synthesis MCR is of biotechnological interest for the synthesis of polyester building blocks Sulfurisphaera tokodaii

Cloned(Commentary)

Cloned (Comment) Organism
Escherichia coli Rosetta 2 cells transformed with pTrc99A-Mcr plasmid harbouring mcr gene from Sulfolobus tokodaii Sulfurisphaera tokodaii

Crystallization (Commentary)

Crystallization (Comment) Organism
malonyl-CoA reductase in the substrate-free state at 2.05 A resolution and in complex with NADP+ at 1.9 A resolution and in complex with CoA at 2.4 A resolution Sulfurisphaera tokodaii
sitting drop method, 18°C Sulfurisphaera tokodaii

Protein Variants

Protein Variants Comment Organism
additional information the crystallographic data indicate how to construct a bispecific cofactor binding site and to engineer a malonyl-CoA into methylmalonyl-CoA reductase for polyester building block production Sulfurisphaera tokodaii

Organism

Organism UniProt Comment Textmining
Sulfurisphaera tokodaii Q96YK1
-
-
Sulfurisphaera tokodaii DSM 16993 Q96YK1
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Sulfurisphaera tokodaii
recombinant enzyme purified by heat precipitation at 85°C and concentration by ultrafiltration, gel filtration chromatography using a Superdex 200 HR 26/60 gel filtration column and Resource phenyl chromatography using a Resource phenyl column Sulfurisphaera tokodaii

Reaction

Reaction Comment Organism Reaction ID
malonate semialdehyde + CoA + NADP+ = malonyl-CoA + NADPH + H+ the protein acts as rigid template to press CoA and NADP into similar S-shaped, superimposable forms Sulfurisphaera tokodaii
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
malonyl-CoA + NADPH + H+
-
 Sulfurisphaera tokodaii malonate semialdehyde + CoA + NADP+
-
 ?
malonyl-CoA + NADPH + H+ structural analysis reveals an unexpected reaction cycle in which NADP+ and CoA successively occupy identical binding sites, proposed reaction mechanism Sulfurisphaera tokodaii malonate semialdehyde + CoA + NADP+
-
 ?
malonyl-CoA + NADPH + H+
-
 Sulfurisphaera tokodaii DSM 16993 malonate semialdehyde + CoA + NADP+
-
 ?
malonyl-CoA + NADPH + H+ structural analysis reveals an unexpected reaction cycle in which NADP+ and CoA successively occupy identical binding sites, proposed reaction mechanism Sulfurisphaera tokodaii DSM 16993 malonate semialdehyde + CoA + NADP+
-
 ?
succinyl-CoA + NADPH + H+
-
 Sulfurisphaera tokodaii succinic semialdehyde + CoA + NADP+
-
 ?
succinyl-CoA + NADPH + H+
-
 Sulfurisphaera tokodaii DSM 16993 succinic semialdehyde + CoA + NADP+
-
 ?

Subunits

Subunits Comment Organism
homotetramer organized as a dimer of two dimers Sulfurisphaera tokodaii

Synonyms

Synonyms Comment Organism
malonyl-CoA reductase
-
 Sulfurisphaera tokodaii
MCR
-
 Sulfurisphaera tokodaii

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Sulfurisphaera tokodaii