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Table 1 Properties of biochemically characterized rubber oxygenases

From: Biochemical and spectroscopic characterization of purified Latex Clearing Protein (Lcp) from newly isolated rubber degrading Rhodococcus rhodochrous strain RPK1 reveals novel properties of Lcp

  LcpRr LcpK30 LcpVH2 a RoxAXsp
Gene length [bp] 1227 1224 1224 2037
Residues (pre-/mature enzyme) 408/378 407/377 407/371a 678/648
Molecular mass (apo-/mature protein) [kDa] 45.2/42.2 44.0/41.0 45.5/41.7a 74.7/71.5
strep tagged [kDa] 44.5 43.3   
pH optimum 8 7 7 7
Molar extinction coefficient [104 M−1 cm−1] 9.5 (407 nm) 8.0 (412 nm) n.d. 20.6 (406 nm)
Metal atoms per protein molecule     
 Fe 0.98 1.16/1.05 n.d. 2.3
 Cu 0.36 0.056/- sub-stoichiometric -
 Mn - - n.d. -
 Ni - 0.12/0.05 n.d. -
 Zn - - n.d. -
 Mg, Ca - n.d. n.d. n.d.
Haeme type b-type b-type not known/no haeme c-type
Oxidation state of haeme iron Fe3+ Fe3+   Fe3+---O2-
UVvis effect upon addition of CO no no   yes
Specific activity [U/mg] (23/30/37 °C) 0.9/3.1/b 1.5/n.d./4.6 1.3/n.d./n.d. n.d./0.48/n.d.
Melting point n.d. 61.5 °C n.d. 54.3 °C
Conserved DUF2236 residuesc     
 R 163 164 161  
 T 167 168 165  
 H 197 198 195  
  1. n.d not determined
  2. - not detectable (below detection limit)
  3. (a) deduced from [8, 9, 15] and SignalP4.1 Server
  4. (b) activities of LcpRr at 37 °C were not reproducible in oxygen consumption assay
  5. (c) position in native sequence