Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.3.1.179 extracted from

  • Zhang, Y.; Hurlbert, J.; White, S.W.; Rock, C.O.
    Roles of the active site water, histidine 303, and phenylalanine 396 in the catalytic mechanism of the elongation condensing enzyme of Streptococcus pneumoniae (2006), J. Biol. Chem., 281, 17390-17399.
    View publication on PubMed
Search for more literature for 2.3.1.179

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant His-tagged FabF in Escherichia coli strain BL21(DE3) Streptococcus pneumoniae

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant mutant H303A from 20% polyethylene glycol 3350, 0.2 M potassium acetate, X-ray diffraction structure determination and analysis Streptococcus pneumoniae

Protein Variants

Protein Variants Comment Organism
C164A site-directed mutagenesis, inactive mutant Streptococcus pneumoniae
C164A/H337A site-directed mutagenesis, inactive mutant Streptococcus pneumoniae
C164A/K332A site-directed mutagenesis, inactive mutant Streptococcus pneumoniae
E346A site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme Streptococcus pneumoniae
E396A site-directed mutagenesis, the mutant shows no condensation activity but retains about 50% of wild-type transacylation activity with acyl-ACP and ACP, and 40% of wild-type decarboxylation activity Streptococcus pneumoniae
H303A site-directed mutagenesis, the mutant shows 74% reduced condensation activity, 40% reduced transacylation activity, and 5fold increased decarboxylation activity, compared to the wild-type enzyme Streptococcus pneumoniae
H337A site-directed mutagenesis, inactive mutant Streptococcus pneumoniae
K332A site-directed mutagenesis, the mutant shows no condensation activity but retains about 30% of wild-type transacylation activity with acyl-ACP and ACP, and 10% of wild-type decarboxylation activity Streptococcus pneumoniae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
myristoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] Streptococcus pneumoniae
-
 ? + CO2 + [acyl-carrier protein]
-
 ?

Organism

Organism UniProt Comment Textmining
Streptococcus pneumoniae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant His-tagged FabF from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Streptococcus pneumoniae

Reaction

Reaction Comment Organism Reaction ID
a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a (Z)-3-oxooctadec-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein] elongation condensing enzyme, catalytic mechanism involving Cys134, His337, and His303, forming the catalytic triad, as well as Phe396, and a water molecule bound to the active site, analysis of residues involved in the different reaction steps, overview Streptococcus pneumoniae
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information analysis of interaction between FabF and the acyl-carrier protein Streptococcus pneumoniae ?
-
 ?
myristoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
-
 Streptococcus pneumoniae ? + CO2 + [acyl-carrier protein]
-
 ?

Synonyms

Synonyms Comment Organism
beta-ketoacyl-ACP synthase II
-
 Streptococcus pneumoniae
FabF
-
 Streptococcus pneumoniae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Streptococcus pneumoniae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8 7 assay at Streptococcus pneumoniae