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Literature summary for 3.5.1.88 extracted from

  • Ngo, H.P.; Ho, T.H.; Lee, I.; Tran, H.T.; Sur, B.; Kim, S.; Kim, J.G.; Ahn, Y.J.; Cha, S.S.; Kang, L.W.
    Crystal structures of peptide deformylase from rice pathogen Xanthomonas oryzae pv. oryzae in complex with substrate peptides, actinonin, and fragment chemical compounds (2016), J. Agric. Food Chem., 64, 7307-7314 .
    View publication on PubMed

Application

Application Comment Organism
drug development the enzyme is an important target to develop antibacterial agents Xanthomonas oryzae pv. oryzae

Cloned(Commentary)

Cloned (Comment) Organism
gene def, sequence comparisons, recombinant expression Xanthomonas oryzae pv. oryzae

Crystallization (Commentary)

Crystallization (Comment) Organism
purified enzyme in complex with product peptides Met-Ala-Ser and Met-Ala, with inhibitor actinonin, and with six fragment chemical compounds bound in the substrate-binding pocket, X-ray diffraction structure determination and analysis at 1.9 A resolution Xanthomonas oryzae pv. oryzae

Inhibitors

Inhibitors Comment Organism Structure
actinonin analysis of the binding structure to XoPDF Xanthomonas oryzae pv. oryzae
additional information actinonin binding structure comparisons of enzymes from different sources Xanthomonas oryzae pv. oryzae

Metals/Ions

Metals/Ions Comment Organism Structure
Cd2+ the metal ion is bound in the active site, metalloprotease, metal binding and coordination structure of enzyme XoPDF Xanthomonas oryzae pv. oryzae
additional information comparisons to Escherichia coli metal binding structures with Co2+ and Fe2+ Xanthomonas oryzae pv. oryzae
Zn2+ the metal ion is bound in the active site, metalloprotease, metal binding and coordination structure of enzyme XoPDF Xanthomonas oryzae pv. oryzae

Organism

Organism UniProt Comment Textmining
Xanthomonas oryzae pv. oryzae Q5H3Z2
-
-
Xanthomonas oryzae pv. oryzae KACC10331 Q5H3Z2
-
-
Xanthomonas oryzae pv. oryzae KXO85 Q5H3Z2
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
formyl-Met-Ala + H2O
-
Xanthomonas oryzae pv. oryzae formate + Met-Ala
-
?
formyl-Met-Ala + H2O
-
Xanthomonas oryzae pv. oryzae KACC10331 formate + Met-Ala
-
?
formyl-Met-Ala + H2O
-
Xanthomonas oryzae pv. oryzae KXO85 formate + Met-Ala
-
?
formyl-Met-Ala-Ser + H2O
-
Xanthomonas oryzae pv. oryzae formate + Met-Ala-Ser
-
?
formyl-Met-Ala-Ser + H2O
-
Xanthomonas oryzae pv. oryzae KACC10331 formate + Met-Ala-Ser
-
?
formyl-Met-Ala-Ser + H2O
-
Xanthomonas oryzae pv. oryzae KXO85 formate + Met-Ala-Ser
-
?

Subunits

Subunits Comment Organism
More enzyme structure analysis Xanthomonas oryzae pv. oryzae

Synonyms

Synonyms Comment Organism
DEF
-
Xanthomonas oryzae pv. oryzae
PDF
-
Xanthomonas oryzae pv. oryzae
XOO1075
-
Xanthomonas oryzae pv. oryzae
XoPDF
-
Xanthomonas oryzae pv. oryzae

General Information

General Information Comment Organism
physiological function peptide deformylase (PDF) catalyzes the removal of the N-formyl group from the N-terminus of newly synthesized polypeptides in bacterial cells Xanthomonas oryzae pv. oryzae