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Literature summary for 1.14.19.58 extracted from

  • Ortega, M.A.; Cogan, D.P.; Mukherjee, S.; Garg, N.; Li, B.; Thibodeaux, G.N.; Maffioli, S.I.; Donadio, S.; Sosio, M.; Escano, J.; Smith, L.; Nair, S.K.; van der Donk, W.A.
    Two flavoenzymes catalyze the post-translational generation of 5-chlorotryptophan and 2-aminovinyl-cysteine during NAI-107 biosynthesis (2017), ACS Chem. Biol., 12, 548-557 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.19.58

Cloned(Commentary)

Cloned (Comment) Organism
gene mibH, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His6-tagged enzyme in Escherichia coli, coexpression of mibH with the chaperones groES/EL and gene mibS Microbispora sp.

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant His6-tagged enzyme with bound FAD, hanging drop vapour diffusion method, mixing of 22 mg/ml protein in 20 mM HEPES, pH 8.0, and 150 mM KCl, with reservoir solution containing 12.5% MPD, 12.5% PEG 3350, 0.1 M MES/imidazole, pH 6.5, and 0.09 M NPS (1:1:1 NaNO3, Na2HPO4, (NH4)2SO4), X-ray diffraction structure determination and analysis at 1.85 A resolution Microbispora sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-tryptophan + FADH2 + Cl- + O2 + H+ Microbispora sp.
-
 5-chloro-L-tryptophan + FAD + 2 H2O
-
 ?
L-tryptophan + FADH2 + Cl- + O2 + H+ Microbispora sp. ATCC PTA-5024
-
 5-chloro-L-tryptophan + FAD + 2 H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Microbispora sp. E2IHC5
-
-
Microbispora sp. ATCC PTA-5024 E2IHC5
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography and gel filtration Microbispora sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-tryptophan + FADH2 + Cl- + O2 + H+
-
 Microbispora sp. 5-chloro-L-tryptophan + FAD + 2 H2O
-
 ?
L-tryptophan + FADH2 + Cl- + O2 + H+
-
 Microbispora sp. ATCC PTA-5024 5-chloro-L-tryptophan + FAD + 2 H2O
-
 ?
lantibiotic NAI-107-[tryptophan] + FADH2 + Cl- + O2 + H+ NAI-107 acts as a peptidoglycan biosynthesis inhibitor by sequestering the cell wall precursor lipid II Microbispora sp. lantibiotic NAI-107-[5-chlorotryptophan] + FAD + 2 H2O
-
 ?
lantibiotic NAI-107-[tryptophan] + FADH2 + Cl- + O2 + H+ NAI-107 acts as a peptidoglycan biosynthesis inhibitor by sequestering the cell wall precursor lipid II Microbispora sp. ATCC PTA-5024 lantibiotic NAI-107-[5-chlorotryptophan] + FAD + 2 H2O
-
 ?
additional information structure-based analysis of the enzyme's substrate specificity, structure-function relationship, overview Microbispora sp. ?
-
 ?
additional information structure-based analysis of the enzyme's substrate specificity, structure-function relationship, overview Microbispora sp. ATCC PTA-5024 ?
-
 ?

Synonyms

Synonyms Comment Organism
mibH
-
 Microbispora sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Microbispora sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Microbispora sp.

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Microbispora sp.

General Information

General Information Comment Organism
evolution structure comparisons reveal subtle amino acid differences within the MibH substrate binding site generates a solvent exposed crevice presumably involved in determining the substrate specificity of this unusual peptide halogenase Microbispora sp.
physiological function MibH is an FADH2-dependent Trp halogenase, that is only active when Trp is embedded within its cognate peptide substrate deschloro NAI-107 Microbispora sp.