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. 1999 Aug 3;96(16):8955–8960. doi: 10.1073/pnas.96.16.8955

Table 1.

Substrate specificity of recombinant sweetgum LsM88 (CAld5H) and LsCOMT (COMT) proteins and of sweetgum xylem proteins

Substrate Substrate specificity (pmol/min per mg protein)
Recombinant proteins
Xylem proteins
CAld5H COMT CAld5H + COMT Microsome Soluble Microsome + soluble
Coniferyl aldehyde 723.9 ± 24.0 382.2 ± 15.2 114.0 ± 3.6 13.8 ± 1.2
(5-OH-CAld) (SAld) (5-OH-CAld) (SAld)
Ferulate 60.7 ± 3.2 32.2 ± 2.4 26.3 ± 1.2 12.0 ± 1.4
(5-OH-FA) (SA) (5-OH-FA) (SA)
5-Hydroxyconiferyl aldehyde 14,370 ± 200 5,900 ± 35
(SAld) (SAld)
5-Hydroxyferulate 12,710 ± 70 5,700 ± 90
(SA) (SA)
526.5 ± 30.0 247.5 ± 17.2 8.8 ± 1.4 4.8 ± 1.9
Coniferyl aldehyde + ferulate (5-OH-CAld) (SAld) (5-OH-CAld) (SAld)
0 0 0 0
(5-OH-FA) (SA) (5-OH-FA) (SA)

Substrate and recombinant protein concentrations and the control experiments were the same as described in Fig. 2. For assaying xylem proteins, 9.5 and 720 μg of soluble and microsome proteins were used, respectively, with the same substrate concentrations as for recombinant proteins and boiled plant proteins as control. Specific activities were mean ± SD (n = two to three independent assays). Reaction products: 5-OH-CAld, 5-hydroxyconiferyl aldehyde; 5-OH-FA, 5-hydroxyferulate; SAld, sinapyl aldehyde; SA, sinapate.