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Literature summary extracted from

  • Kuessau, T.; Flipo, M.; Van Wyk, N.; Viljoen, A.; Olieric, V.; Kremer, L.; Blaise, M.
    Structural rearrangements occurring upon cofactor binding in the Mycobacterium smegmatis ?-ketoacyl-acyl carrier protein reductase MabA (2018), Acta Crystallogr. Sect. D, 74, 383-393 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.100 expressed in Escherichia coli BL21 Rosetta 2 (DE3) pLysS cells Mycolicibacterium smegmatis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.100 high-resolution crystal structures of the enzyme (MabA) in its apo, NADP+-bound and NADPH-bound forms. Crystals are grown in sitting drops in MR Crystallization Plates (Hampton Research) at 18°C Mycolicibacterium smegmatis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.100 0.6
-
 3-oxooctanoyl-CoA pH 7.0, 25°C Mycolicibacterium smegmatis
1.1.1.100 3.5
-
 acetoacetyl-CoA pH 7.0, 25°C Mycolicibacterium smegmatis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.100 133000
-
 tagged enzyme form, gel filtration Mycolicibacterium smegmatis

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.100 Mycolicibacterium smegmatis P71534
-
-
1.1.1.100 Mycolicibacterium smegmatis ATCC 700084 P71534
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.100
-
 Mycolicibacterium smegmatis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.100 3-oxooctanoyl-CoA + NADPH numerous residues trigger steric hindrance to the binding of NADPH and substrate. Upon NADPH binding, these residues are pushed away from the active site, allowing the enzyme to adopt an open conformation. The transition from an NADPH-bound to an NADP+-bound form is likely to facilitate release of the product Mycolicibacterium smegmatis (R)-3-hydroxyoctanoyl-CoA + NADP+
-
 ?
1.1.1.100 3-oxooctanoyl-CoA + NADPH numerous residues trigger steric hindrance to the binding of NADPH and substrate. Upon NADPH binding, these residues are pushed away from the active site, allowing the enzyme to adopt an open conformation. The transition from an NADPH-bound to an NADP+-bound form is likely to facilitate release of the product Mycolicibacterium smegmatis ATCC 700084 (R)-3-hydroxyoctanoyl-CoA + NADP+
-
 ?
1.1.1.100 acetoacetyl-CoA + NADPH + H+ numerous residues trigger steric hindrance to the binding of NADPH and substrate. Upon NADPH binding, these residues are pushed away from the active site, allowing the enzyme to adopt an open conformation. The transition from an NADPH-bound to an NADP+-bound form is likely to facilitate release of the product Mycolicibacterium smegmatis 3-hydroxybutyryl-CoA + NADP+
-
 ?
1.1.1.100 acetoacetyl-CoA + NADPH + H+ numerous residues trigger steric hindrance to the binding of NADPH and substrate. Upon NADPH binding, these residues are pushed away from the active site, allowing the enzyme to adopt an open conformation. The transition from an NADPH-bound to an NADP+-bound form is likely to facilitate release of the product Mycolicibacterium smegmatis ATCC 700084 3-hydroxybutyryl-CoA + NADP+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.100 homotetramer
-
 Mycolicibacterium smegmatis

Synonyms

EC Number Synonyms Comment Organism
1.1.1.100 beta-ketoacyl-acyl carrier protein reductase
-
 Mycolicibacterium smegmatis
1.1.1.100 MabA
-
 Mycolicibacterium smegmatis
1.1.1.100 MSMEG_3150
-
 Mycolicibacterium smegmatis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.100 0.019
-
 acetoacetyl-CoA pH 7.0, 25°C Mycolicibacterium smegmatis
1.1.1.100 0.095
-
 3-oxooctanoyl-CoA pH 7.0, 25°C Mycolicibacterium smegmatis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.100 NADPH numerous residues trigger steric hindrance to the binding of NADPH and substrate. Upon NADPH binding, these residues are pushed away from the active site, allowing the enzyme to adopt an open conformation. The transition from an NADPH-bound to an NADP+-bound form is likely to facilitate release of the product Mycolicibacterium smegmatis