By Professor Dr. Dietmar Schomburg, Dr. Dörte Stephan (auth.), Professor Dr. Dietmar Schomburg, Dr. Dörte Stephan (eds.)
Today, because the huge overseas genome series initiatives are gaining a large amount of public consciousness and enormous series facts bases are created or not it's comes an increasing number of visible that we're very restricted in our skill to entry useful info for the gene items -the proteins, specifically for enzymes. these info are inherently very tough to assemble, interpret and standardize as they're hugely allotted between journals from diversified fields and are frequently sub ject to experimental stipulations. however a scientific assortment is key for our interpretation of the genome info and extra so for attainable appli cations of that wisdom within the fields of medication, agriculture, and so on .. contemporary professional gress on enzyme immobilization, enzyme construction, enzyme inhibition, coen zyme regeneration and enzyme engineering has unfolded attention-grabbing new fields for the capability software of enzymes in a wide variety of other components. it's the sensible profile of an enzyme that allows a biologist of medical professional to research a metabolic pathway and its disturbance; it's the substrate specificity of an enzyme which tells an analytical biochemist the way to layout an assay; it's the balance, specificity and potency of an enzyme which determines its usefulness within the biotechnical transformation of a molecule. And the sum of a lot of these information must be thought of while the dressmaker of synthetic biocatalysts has to settle on the optimal prototype to begin with.
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Extra info for Enzyme Handbook: 14: Class 2.7–2.8 Transferases, EC 2.7.1.105–EC 2.8.3.14
Sample text
11]. can replace Mg2+ [2] or Zn 2+ [11] to some extent [2. 11]. inhibitory above 6 mM [7]. 3]) [2. 11]; Mn 2+ (activation. can replace Ca2+ to some extent [6]. inhibitory above 6 mM [7]. not [10]) [5-7]; Zn 2+ (activation. most effective [11]. can replace Ca2+ to some extent [6]. inhibitory [7]) [6. 10. 11]; C02+ (activation. 5 mM [7]. can replace Zn 2+ to some extent [11]. 11]; Cd 2+ (slight activation) [11]; Fe 2+ (slight activation) [11]; Sr2+ (slight activation) [11]; Ni 2+ (slight activation) [11]; More (no activation by exogenous divalent metal ions) [1.
BioI. : BioI. Chem. : J. BioI. : Eur. J. : Proc. Natl. Acad. Sci. : Eur. J. : Proc. Natl. Acad. Sci. : J. BioI. : Biochem. Biophys. Res. Verlag Berlin Heidelberg 1997 Duplication. 110 Systematic name ATP:dephospho[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase] phosphotransferase Recommended name Dephospho-[reductase kinase] kinase Synonyms Kinase (phosphorylating), hydroxymethylglutaryl coenzyme A reductase kinase Reductase kinase kinase AMP-activated protein kinase kinase Hydroxymethylglutaryl coenzyme A reductase kinase kinase CAS Reg.
Acad. Sci. : Eur. J. : Proc. Natl. Acad. Sci. : J. BioI. : Biochem. Biophys. Res. Verlag Berlin Heidelberg 1997 Duplication. 110 Systematic name ATP:dephospho[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase] phosphotransferase Recommended name Dephospho-[reductase kinase] kinase Synonyms Kinase (phosphorylating), hydroxymethylglutaryl coenzyme A reductase kinase Reductase kinase kinase AMP-activated protein kinase kinase Hydroxymethylglutaryl coenzyme A reductase kinase kinase CAS Reg. No.
