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journal homepage: www.elsevier.com/locate/soilbio

Short communication

Gangsheng Wang*, Wilfred M. Post

Climate Change Science Institute and Environmental Sciences Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831-6301, USA

a r t i c l e i n f o

a b s t r a c t

Article history:

Received 1 June 2012

Received in revised form

27 August 2012

Accepted 29 August 2012

Available online 13 September 2012

We theoretically derived a general equation describing the enzyme kinetics that could be further

simplied to the typical MichaeliseMenten (MeM) kinetics or the reverse MeM equation (RMeM)

under the condition of S z S1 >> E0 or S1 << E0, respectively, where E0 and S1 ( S ES) are the

concentrations of total enzyme and substrate including free substrate (S) and enzymeesubstrate

complex (ES). We showed that the related Schimel and Weintraub RMeM equation (RMeMeSW) can

be derived from the Langmuir adsorption isotherm theory with S >> E0. Both the MeM and the RM-MSW are appropriate to eld soil conditions with S >> E0 given different values of specic reaction rate

(k3) and half-saturation constant (Ks). In contrast to MeM and RMeMeSW models, the RMeM model is

not applicable to eld conditions because of its limited application to one substrate with a simple

enzyme system. However, we demonstrate that the best formulation for the process of enzyme-mediated

decomposition may vary depending on whether the process is limited by substrate or enzyme

availability.

Published by Elsevier Ltd.

Keywords:

Enzyme kinetics

Langmuir adsorption isotherm

MichaeliseMenten kinetics

Reverse MichaeliseMenten kinetics

Sensitivity

1. Introduction

Soil enzymes have been explicitly included in the modeling of

soil organic matter (SOM) dynamics (Lawrence et al., 2009). In

addition to the MichaeliseMenten (MeM) kinetics (Allison et al.,

2010; Wang et al., in press), the reverse MichaeliseMenten model

(RMeMeSW) proposed by Schimel and Weintraub (2003) has been

used to describe soil enzyme kinetics. The RMeMeSW kinetics

functionally reverses the dependency of the MeM equation on

substrate availability (Schimel and Weintraub, 2003). The size of

the SOM pool in the RMeMeSW is assumed to be sufciently large

so that the amount of enzyme, rather than substrate, is the ratelimiting factor for SOM decomposition (Lawrence et al., 2009;

Moorhead and Sinsabaugh, 2006; Schimel and Weintraub, 2003).

The typical MeM and the RMeMeSW can be expressed by Eqs. (1)

and (2), respectively

q This manuscript has been authored by UT-Battelle, LLC, under Contract No. DEAC05-00OR22725 with the U.S. Department of Energy. The United States Government retains and the publisher, by accepting the article for publication, acknowledges that the United States Government retains a non-exclusive, paid-up,

irrevocable, world-wide license to publish or reproduce the published form of this

manuscript, or allow others to do so, for United States Government purposes.

* Corresponding author. Bldg 2040, Room E272, MS-6301, Oak Ridge National

Laboratory, Oak Ridge, TN 37831-6301, USA.

E-mail address: wangg@ornl.gov (G. Wang).

0038-0717/$ e see front matter Published by Elsevier Ltd.

http://dx.doi.org/10.1016/j.soilbio.2012.08.028

vM

k3;M $E0 $S

Ks;M S

(1)

vR

k3;R $E0 $S

Ks;R E0

(2)

where the subscript M and R in v, k3, and Ks denote the MeM and

RM-M-SW kinetics, respectively; E0 and S represent the concentration of total enzyme and free substrate, respectively; v is the

SOM decomposition rate; k3 denotes the specic rate constant and

k3,M in Eq. (1) is equivalent to the turnover number (kcat) (Johnson

and Goody, 2011); Ks denotes the half-saturation constant. Mathematically, the RMeMeSW (Eq. (2)) uses the enzyme pool instead

of the substrate pool in the denominator of the typical MeM

equation (Eq. (1)).

This RMeMeSW formulation is different from the reverse

MichaeliseMenten equation described in Bowie et al. (1985). The

rate-limitation term of Bowie et al. (1985) has the form of Ks/

(Ks S) rather than S/(Ks S) as in the typical MeM equation. As

stated by Schimel and Weintraub (2003), the adoption of the

nonlinear RMeMeSW kinetics makes it possible to construct

a stable system by providing a saturating response, while the rstorder enzyme kinetics could result in an unstable microbial

biomass pool in their C-only model because of a lack of nonlinear

kinetics. Actually, the rst-order kinetics used by Schimel and

Weintraub (2003) is a simplication of the MeM equation since

invariant, i.e., S/(Ks,M S) in Eq. (1) becomes constant.

The MeM kinetics is theoretically derivable for a simple enzyme

with only one active site and a single substrate (Briggs and Haldane,

1925; Johnson and Goody, 2011). The RMeMeSW model was

introduced as an empirical equation rather than one derived on

a theoretical basis (Schimel and Weintraub, 2003). In this paper, we

provided theoretical derivations of the enzyme kinetics models and

elaborated under what conditions these models are valid.

Robson and Garnier (1986) referred to the total substrate (denoted

by S0) in the left side of Eq. (11) since the enzyme concentration was

considered to be signicant compared to substrate concentration

and the product concentration (P) was negligible in their case

(Easterby, 1981; Leskovac, 2003). We can replace v with Vmax/2 and

solve for S1 in Eq. (11) to provide an estimate of the apparent halfsaturation concentration of S1

app

Ks

2. Derivation of the reverse MichaeliseMenten equation

k1

k3

k2

(3)

respectively, ES is the intermediate enzymeesubstrate complex

which reacts to form the product P, and results in the release of the

enzymes (E). The rate constants k1 and k3 denote the forward

reactions, and the rate constant k2 refers to a reverse reaction

(Johnson and Goody, 2011).

One of the important assumptions in the MeM kinetics is that

the concentration of intermediate species (ES) is quasi-steady, i.e.,

the rate of production of ES equals the rate of degradation of ES

(Briggs and Haldane, 1925). This assumption yields

E$S Ks $ES

(4)

substrate concentration at which the reaction rate v Vmax/2; and

Vmax is the maximum reaction rate.

The reaction (production) rate is proportional to the concentration of ES:

v dP=dt k3 $ES

(5)

condition that all enzyme (E0) is converted to ES:

Vmax k3 $E0

(6)

where E0 consists of two forms, i.e., the free enzyme (E) and the

enzymeesubstrate complex (ES):

E0 E ES

(13)

where A Ks E0 S1 and B 4E0$S1. Since A2 e

B (Ks)2 2$Ks$(E0 S1) (E0 S1)2 > 0, B/A2 < 1, i.e.,

(14)

Moller et al., 1997) and Eq. (14), the truncated rst-order approximation to the square root in Eq. (13) can be expressed as

p

A2 BzA B=2A

(15a)

It follows that

A

p

A2 BzB=2A 2E0 $S1 =Ks E0 S1

(15b)

Substituting Eq. (15b) into Eq. (13) with Vmax k3$E0 from Eq.

(6) yields

Vmax $S1

k3 $E0 $S1

vz

Ks E0 S1

Ks E0 S1

(16)

replacing v with Vmax/2 and solving S1. Equation (16) may be further

simplied into:

(8)

k $E $S

vz 3 0 1 ; if S1 << E0

Ks E0

(17b)

(9)

(10)

Replacing ES in Eq. (10) with Eq. (8) and rearranging Eq. (10)

yield

S1 Ks $v=Vmax v E0 $v=Vmax

q

v Vmax =2E0 $ Ks E0 S1 Ks E0 S1 2 4E0 $S1

p

Vmax =2E0 $ A A2 B

(17a)

respectively, Eq. (4) becomes

E0 ES$S1 ES Ks $ES

where Ks

is called the apparent or effective Ks by Robson and

Garnier (1986). The Ksapp is dependent on enzyme concentration

and larger than the intrinsic half-saturation constant (Ks).

The solution to Eq. (11) for v is

k $E $S

k $E $S

vz 3 0 1 z 3 0 ; if S1 >>E0

Ks S

Ks S1

We dene S1 as the sum of the free substrate and the enzymebound substrate:

S1 S ES

(12)

(7)

ES E0 $v=Vmax

S1 jvVmax =2 Ks E0 =2

app

(Johnson and Goody, 2011; Leskovac, 2003):

S E % ES / E P

947

(11)

Garnier (1986). However, S1 in our formula denotes the sum of the

Equations (16) and (17a,b) indicate that (i) under the condition

of S1 >> E0, the reaction rate can be expressed by the typical MeM

kinetics since S z S1 (Eq. (17a) equivalent to Eq. (1)); (ii) in the case

of S1 << E0, the reaction rate (Eq. (17b)) has a similar formulation to

the RMeMeSW equation (Eq. (2)); for convenience, we named Eq.

(17b) as the RMeM equation to distinguish it from the RMeMeSW;

and (iii) when the enzyme concentration is comparable to the

substrate concentration, both S1 and E0 should be included in the

denominator as indicated by Eq. (16).

The above derivation is appropriate for a simple enzyme and

a single substrate. However, there are many enzymes competing for

the binding sites on a broad range of insoluble substrates in soils

(Schimel and Weintraub, 2003). The limiting factor is the availability of effective binding sites on solid substrates (Sinsabaugh and

948

Table 1

Comparisons of three models: MichaeliseMenten (MeM), reverse MeM (RMeM) and Schimel and Weintraub RMeM (RMeMeSW).

MeM

Equationa

Theoretical basis

Assumption

More sensitive to enzyme

than to substrate

Applications

RMeM

k3;M $E0 $S

vM

Ks;M S

Enzyme catalysis as a chain reaction

S z S1 >> E0

Yes

Simple enzyme/single substrate;

many enzymes/complex substrates

RMeMeSW

S1 << E0

No

k3;R $E0 $S

Ks;R E0

Langmuir adsorption isotherm theory

S >> E0

No

vRM

Ks;M E0

vR

a

Mathematical equations for different models, E0 and S represent the concentration of total enzyme and free substrate, respectively; S1 S ES, where ES is the

concentration of enzymeesubstrate complex; v is the reaction rate; k3 denotes the maximum specic rate constant; Ks denotes the half-saturation constant; and the subscript

in v, k3, and Ks denote different models.

can use a formulation analogous to the Langmuir equation (Sohn

and Kim, 2005) to estimate the fraction of binding sites with the

enzyme as the adsorbate:

KBA $E0

1 KBA $E0

(18)

binding sites occupied to the number of available sites) and KBA is

the binding afnity. If we assume that (i) the maximum binding

capacity is proportional to the concentration of substrate (S) and (ii)

the decomposition rate (vR) is proportional to the binding amount

of enzyme, vR can be estimated as

KBA $E0

a$E0 $S

vR a$q$S a$

$S

1=KBA E0

1 KBA $E0

(19)

account the aforementioned two assumptions. Eq. (19) is equivalent to Eq. (2) if a and 1/KBA are replaced by k3,R and Ks,R, respectively. Therefore, the RMeMeSW can be derived from the Langmuir

adsorption isotherm theory.

3. Model comparisons

A summary of the model comparisons is shown in Table 1. The

MeM and the RMeM are theoretically derived for a simple enzyme

and a single substrate under opposite conditions in terms of the

concentrations of enzyme and substrate. When the system is

substrate limited (S1 << E0), the RMeM is valid. The MeM equation

does not literally apply to complex systems such as SOM

(Sinsabaugh and Osgood, 2007). The derived k3 and Ks by tting the

v w S relationship from laboratory experiments with a simple

enzyme and a single substrate cannot be directly used for eld soil

conditions (Wang et al., 2012). In ecosystems, the parameters (k3

and Ks) of the MeM model are often not independent and are

functions of the methods and conditions of measurement

(Sinsabaugh and Osgood, 2007). The RMeMeSW may be derived

from the Langmuir adsorption isotherm theory, which is theoretically based on the statistical rate theory of interfacial transport

(Rudzinski and Panczyk, 2000; Ward et al., 1982). While RMeM is

supercially similar to the RMeMeSW, the RMeM is actually

different in principle from the RMeMeSW since the latter is

applicable under enzyme-limited conditions (S >> E0). In addition,

as shown from our derivation, most of the substrate is bound to the

enzyme and S1 in the RMeM (Eq. (17b)) may not be changeable

with S when S1 << E0.

Is the reaction rate more sensitive to changes in enzyme

concentration than to changes in substrate concentration when the

system is enzyme-limited (S >> E0)? To answer this question we

conducted a sensitivity analysis of both the MeM and the RM-MSW equations. Following the approach of Wang and Post (2012),

the sensitivities of the reaction rate (vM) in the MeM kinetics to the

changes in the concentrations of enzyme (E0) and substrate (S) are

vvM vM

k3;M $S$E0

vE

E0

Ks;M S vM

0

(20a)

vvM vM

k3;M S$E0

Ks;M $

$

vS

S

Ks;M S Ks;M S vM

(20b)

(vR) to changes in E0 and S are

vvR vR

k3;R

Ks;R

S$E0

$

$

vE

E0

Ks;R E0 Ks;R E0 vR

0

(21a)

vvR vR

k3;R

S$E0

$

vS

S

Ks;R E0 vR

(21b)

respectively.

Eq. (20a) and (20b) indicate that, with the same S and E0 values,

the reaction rate (vM) of the MeM model is more sensitive to the

changes in enzyme concentration (E0) than to the changes in S since

Ks,M/(Ks,M S) < 1 regardless of the concentrations of S and E0. On

the contrary, vR of the RMeMeSW model is more sensitive to the

changes in S than to the changes in E0 because of Ks,R/(Ks,R E0) < 1.

Similarly, the RMeM model is more sensitive to substrate than to

enzyme. The above analysis indicates that the relative sensitivities

of the three models are independent of the relative sizes of S and E0.

It also implies that the relative sensitivity of a response variable to

a dependent variable is determined by the response mechanism.

Both the MeM and RMeMeSW have been shown to be useful in

simulating SOM dynamics (Allison et al., 2010; Schimel and

Weintraub, 2003) with S >> E0 and appropriate values of k3 and

Ks. It is possible for the reaction rates for both formulations to be the

same. This occurs when k3,M/(Ks,M S) k3,R/(Ks,R E0) (see Eqs. (1)

and (2)). However, the sensitivities of the reaction rates to enzyme

or substrate availabilities are quite different. Under the condition of

k3,M/(Ks,M S) k3,R/(Ks,R E0), when the MeM is used, the reaction

rate is more sensitive to enzyme concentration (E0) than when the

RMeMeSW is used since Ks,R/(Ks,R E0) < 1 resulting in Eq.

(20a) > Eq. (21a).

4. Conclusion

Both the MeM and the RMeMeSW models are ecologicallyapplicable. The MeM kinetics is theoretically derivable for

a simple enzyme with only one active site and a single substrate

(Briggs and Haldane, 1925; Johnson and Goody, 2011). When the

MeM model is used to model SOM dynamics with many enzymes

and complex substrates, it is an empirical analogy rather than

a theoretical model. The RMeMeSW can be derived from the

Langmuir adsorption isotherm theory. The derivation of the RMeM

equation requires assumptions that are contrary to those required

for RMeMeSW, which limits the applicability of the RMeM to eld

soil conditions. We demonstrate that the best formulation for the

process of enzyme-mediated decomposition may vary depending

on whether the process is limited by substrate or enzyme

availability.

Acknowledgments

Research sponsored by the Laboratory Directed Research and

Development Program of Oak Ridge National Laboratory, managed

by UT-Battelle, LLC, for the U.S. Department of Energy under

contract No. DE-AC05-00OR22725. The authors thank Dr. Xiaojuan

Yang for her technical comments. The authors are also grateful for

the constructive comments and suggestions from the three anonymous reviewers.

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