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Literature summary extracted from

  • Kamo, M.; Kudo, N.; Lee, W.C.; Motoshima, H.; Tanokura, M.
    Crystallization and preliminary X-ray crystallographic analysis of peptide deformylase from Thermus thermophilus HB8 (2004), Acta Crystallogr. Sect. D, 60, 1299-1300.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.88 into pET-vector for expression in Escherichia coli strain BL21(DE3) Thermus thermophilus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.88 by the hanging drop vapour-diffusiuon method using PEG 4000 as a precipitant Thermus thermophilus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.88 Fe2+ Ni2+ or Co2+ leads to the retention of almost full catalytic activity Thermus thermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.88 formyl-L-methionyl peptide + H2O Thermus thermophilus
-
 formate + methionyl peptide
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.88 Thermus thermophilus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.88 using a TSKgel Blue 5pw column, a Mono Q 10/10 column and a Bio-Scale CHT10-I column Thermus thermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.88 formyl-L-methionyl peptide + H2O
-
 Thermus thermophilus formate + methionyl peptide
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.1.88 PDF
-
 Thermus thermophilus
3.5.1.88 peptide deformylase
-
 Thermus thermophilus