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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