Enzyme kinetics: Michaelis-Menten rates and temperature response

How extracellular enzyme rates follow Michaelis-Menten saturation with substrate and Arrhenius-type rise with temperature. Sets the speed at which polymers are cut into units microbes can absorb.

Boundary: where this process starts

Starts with: Enzyme binds substrate and releases product at rate V = Vmax[S]/(Km+[S])

Boundary: where it ends

Ends after: Ecoenzymatic stoichiometry: matching enzymes to nutrient limitation

PARTICIPANTSRESOURCESExtracellularenzymesDecomposersCellulasesPhosphatasesTemperatureCelluloseEnzymesCarbonTemperatureClay mineralsImpact +3 of 5. Click for details and evidence.BindingImpact 03 of 5. Click for details and evidence.Impact +3 of 5. Click for details and evidence.55% substrate far below KmImpact +3 of 5. Click for details and evidence.30% substrate near KmImpact 02 of 5. Click for details and evidence.15% substrate far above KmImpact +3 of 5. Click for details and evidence.Impact +3 of 5. Click for details and evidence.Impact +2 of 5. Click for details and evidence.Impact -3 of 5. Click for details and evidence.Impact -2 of 5. Click for details and evidence.Mineral sorption alters kineImpact +3 of 5. Click for details and evidence.Products accumulateImpact +1 of 5. Click for details and evidence.Impact -3 of 5. Click for details and evidence.↻ balances · moderate · 0.3 Product repressiImpact +3 of 5. Click for details and evidence.Resource limitation steers iImpact +3 of 5. Click for details and evidence.Hydrolysis rate setEnzyme binds substrate and releases product at rate V = Vmax[S]/(Km+[S]): uses up Celluloseuses upEnzyme binds substrate and releases product at rate V = Vmax[S]/(Km+[S]): uses EnzymesSubstrate concentration relative to Km: uses CelluloseSubstrate concentration relative to Km: uses CarbonSubstrate-limited: rate rises roughly in proportion to substrate or enzyme density: uses CelluloseNear Km: rate rises with substrate but with diminishing return: uses CelluloseSaturated: rate capped at Vmax, extra substrate has no effect: uses CelluloseWarming raises Vmax (Q10 about 1.5-2.5 for hydrolases) and also raises Km: uses EnzymesWarming raises Vmax (Q10 about 1.5-2.5 for hydrolases) and also raises Km: uses TemperatureAt low substrate, higher Km reduces the warming gain so temperature sensitivity of decomposition falls: uses CarbonSorption to clay and organic coatings raises apparent Km and lowers apparent Vmax: uses EnzymesSorption to clay and organic coatings raises apparent Km and lowers apparent Vmax: uses Clay mineralsHydrolysis products accumulate and repress further enzyme synthesis (catabolite repression): uses EnzymesEcoenzymatic stoichiometry: matching enzymes to nutrient limitation: uses Carbonbound and hydrolysedCellulose: bound and hydrolysedbind substrate, releaseproductEnzymes: bind substrate, release productconcentration setrelative to KmCellulose: concentration set relative to Kmavailability determinesrate regimeCarbon: availability determines rate regimerate scales with supplyCellulose: rate scales with supplydiminishing returns nearKmCellulose: diminishing returns near Kmextra supply has noeffectCellulose: extra supply has no effectKm rises as wellEnzymes: Km rises as wellraises Vmax with warmingTemperature: raises Vmax with warmingwarming gain reduced atlow substrateCarbon: warming gain reduced at low substrateapparent Km increasesEnzymes: apparent Km increasessorb enzymes, reducingactivityClay minerals: sorb enzymes, reducing activitysynthesis repressed byproductsEnzymes: synthesis repressed by productsinvestment matched todemandCarbon: investment matched to demandStart: Enzyme meetssubstrateSTARTStart: Enzyme meets substrateEnd: Hydrolysis ratesetENDEnd: Hydrolysis rate setEnzyme binds substrateand releases product atrate V…📄1Enzyme binds substrate and releases product at rate V = Vmax[S]/(Km+[S])Substrate concentrationrelative to Km📄1Substrate concentration relative to KmSubstrate-limited: raterises roughly inproportion to substra…📄1Substrate-limited: rate rises roughly in proportion to substrate or enzyme densityNear Km: rate riseswith substrate but withdiminishing return📄1Near Km: rate rises with substrate but with diminishing returnSaturated: rate cappedat Vmax, extrasubstrate has no effect📄1Saturated: rate capped at Vmax, extra substrate has no effectWarming raises Vmax(Q10 about 1.5-2.5 forhydrolases) and al…👍1📄2Warming raises Vmax (Q10 about 1.5-2.5 for hydrolases) and also raises KmAt low substrate,higher Km reduces thewarming gain …📄2At low substrate, higher Km reduces the warming gain so temperature sensitivity of decomposition fallsSorption to clay andorganic coatings raisesapparent Km and lowe…📄1Sorption to clay and organic coatings raises apparent Km and lowers apparent VmaxHydrolysis productsaccumulate and repressfurther enzy…📄2Hydrolysis products accumulate and repress further enzyme synthesis (catabolite repression)Ecoenzymaticstoichiometry: matchingenzymes to nutrie…↘📄1Ecoenzymatic stoichiometry: matching enzymes to nutrient limitation
Line thickness = size of impact (1 to 5)% on a line = chance a fork takes that branch📄 = pieces of evidence on a stepNegative effectLoops backHypothesisResource used up (arrow into the step)Resource used, not used upResource made or released (arrow out of the step)
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Participant
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Resource
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Step
One thing that happens in a process. Every step has at least one participant and carries evidence.
Decision fork
A step where the process can go several ways. Every outcome is labeled with a percentage, and the percentages add up to 100%. It is not limited to yes or no.
Loop
A line that carries the process back to an earlier step. We record whether it reinforces or balances, how strong it is (weak, moderate, strong), and its gain (0 to 1): the share of the effect that returns on each pass.
Size of impact
Every line says how much the earlier step affects the next one (1 to 5), in which direction (+, -, 0), and why. Thicker lines mean bigger impact.
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Boundary
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Description
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Hypothesis
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Inside this process

Every step, with its evidence

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Enzyme binds substrate and releases product at rate V = Vmax[S]/(Km+[S])
Evidence (1) · added by Ember
  • German et al. 2011, Optimization of hydrolytic and oxidative enzyme methods for ecosystem studies, Soil Biol Biochem 43:1387-1397: Soil hydrolase assays fit this relation; Km of beta-glucosidase and phosphatase in the micromolar to hundreds of micromolar range (confidence 0.7)
⑂ Substrate concentration relative to Km
Evidence (1) · added by Ember
  • German, Marcelo, Stone & Allison 2012, The Michaelis-Menten kinetics of soil extracellular enzymes in response to temperature, Global Change Biology 18:1468-1479: Soil substrate near enzymes is often below Km so rate is substrate-limited; shares are estimates (confidence 0.45)
Substrate-limited: rate rises roughly in proportion to substrate or enzyme density
Evidence (1) · added by Ember
  • Burns et al. 2013, Soil enzymes in a changing environment: current knowledge and future directions, Soil Biol Biochem 58:216-234: Review: enzyme activity in soil is usually limited by substrate access, not by enzyme quantity (confidence 0.6)
Near Km: rate rises with substrate but with diminishing return
Evidence (1) · added by Ember
  • German et al. 2011, Optimization of hydrolytic and oxidative enzyme methods for ecosystem studies, Soil Biol Biochem 43:1387-1397: Michaelis-Menten curve between linear and saturated regions (confidence 0.6)
Saturated: rate capped at Vmax, extra substrate has no effect
Evidence (1) · added by Ember
  • German et al. 2011, Optimization of hydrolytic and oxidative enzyme methods for ecosystem studies, Soil Biol Biochem 43:1387-1397: Vmax is the ceiling rate at saturating substrate (confidence 0.7)
Warming raises Vmax (Q10 about 1.5-2.5 for hydrolases) and also raises Km
Evidence (2) · added by Ember
  • German, Marcelo, Stone & Allison 2012, The Michaelis-Menten kinetics of soil extracellular enzymes in response to temperature, Global Change Biology 18:1468-1479: Vmax and Km of soil enzymes both increased with temperature, Km increases partly offset gains (confidence 0.8)
  • Davidson & Janssens 2006, Temperature sensitivity of soil carbon decomposition and feedbacks to climate change, Nature 440:165-173: Decomposition Q10 near 2 typical but varies with substrate quality (confidence 0.7)
At low substrate, higher Km reduces the warming gain so temperature sensitivity of decomposition falls
Evidence (2) · added by Ember
  • German, Marcelo, Stone & Allison 2012, The Michaelis-Menten kinetics of soil extracellular enzymes in response to temperature, Global Change Biology 18:1468-1479: Km rise offsets Vmax rise at low substrate concentrations (confidence 0.65)
  • Allison, Wallenstein & Bradford 2010, Soil-carbon response to warming dependent on microbial physiology, Nature Geoscience 3:336-340: Models with enzyme kinetics predict only transient soil carbon loss under warming (confidence 0.6)
Sorption to clay and organic coatings raises apparent Km and lowers apparent Vmax
Evidence (1) · added by Ember
  • Burns et al. 2013, Soil enzymes in a changing environment: current knowledge and future directions, Soil Biol Biochem 58:216-234: Immobilized enzymes show changed kinetic parameters and extended persistence (confidence 0.65)
Hydrolysis products accumulate and repress further enzyme synthesis (catabolite repression)
Evidence (2) · added by Ember
  • Schimel & Weintraub 2003, The implications of exoenzyme activity on microbial carbon and nitrogen limitation in soil, Soil Biol Biochem 35:549-563: Model: microbes regulate enzyme production according to product availability (confidence 0.6)
  • Allison & Vitousek 2005, Responses of extracellular enzymes to simple and complex nutrient inputs, Soil Biol Biochem 37:937-944: Simple nutrient additions repress some enzyme activities (confidence 0.55)
↘ Ecoenzymatic stoichiometry: matching enzymes to nutrient limitation
Evidence (1) · added by Ember
  • Sinsabaugh et al. 2008, Stoichiometry of soil enzyme activity at global scale, Ecology Letters 11:1252-1264: Global analysis of soil enzyme activity ratios relative to C:N:P of microbial biomass (confidence 0.9)