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The ADP glucose-based starch metabolic pathway contains all the steps, characteristic of plants and C. reinhardtii, with multiple enzyme forms for each pathway step.
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One additional source of information is protein structure, which we, and others, have used successfully to predict the substrates of enzymes, including multiple enzymes forming a pathway by metabolite docking.
E'Hg and E'HgS are inactive enzyme forms.
Each of these protein families often includes multiple enzyme activities.
However, most drugs are metabolized my multiple enzyme pathways.
Although a simplistic model for substrate inhibition proposes binding of two substrate molecules to an enzyme to form an ES2 complex, in many instances, however, substrate inhibition involves a more complex mechanism that includes slow-transition between multiple enzyme species in solution.
The latter (approximately 70 ~ 80% of starch) is a much larger molecule with frequent α-(1 6) branches formed by multiple enzymes, for example, starch synthases (SSs) and starch branching enzymes (SBEs) (Tetlow et al. 2004; Hannah and James 2008).
There are multiple enzymes that convert DAG to other chemical forms.
PDH complexes from prokaryotes and eukaryotes, which have molecular weights in excess of 10 Da, are formed by noncovalent interactions between multiple enzymes.
Our model allows for multiple enzymes and co-substrates, and results in a closed-form analytical expression for the steady-state current response of the disk ultramicroelectrode.
The pathways formed in this process diverge when a glycan is a substrate for multiple enzymes, or converge when multiple glycan substrates all lead to the same product.
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