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Literature summary for 1.1.1.100 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
Search for more literature for 1.1.1.100

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Mycolicibacterium smegmatis P71534
-
-
Mycolicibacterium smegmatis ATCC 700084 P71534
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Mycolicibacterium smegmatis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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+
-
 ?
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+
-
 ?
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+
-
 ?
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

Subunits Comment Organism
homotetramer
-
 Mycolicibacterium smegmatis

Synonyms

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

Turnover Number [1/s]

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

Cofactor

Cofactor Comment Organism Structure
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