Enzyme number

This enzyme [EC 4.6.1.4], also known as 5-enolpyruvyl-shikimate-3-phosphate phospholyase, catalyzes the conversion of 5-0-(l-carboxyvinyl)-3-phosphoshikimate to chorismate and orthophosphate, ft should be noted that shikimate is numbered so that the double bond is between Cl and C2. However, some of the early reports on this enzyme numbered shikimate in the reverse direction. 

Reactions of the hexose monophosphate pathway. Enzymes numbered above are 1) glucose 6-phosphate dehydrogenase and 6-phosphogluconolactone hydrolase, 2) 6-phosphogluconate dehydrogenase,... 

Enzyme Number of Inverting Glycosyl- Nucleophile Electrophile... 

The third figure of the code number, indicating ihc suh-suh class, shows for the oxidoreduciases the type of acceptor involved for the transferases and hydrolases, it stums more precisely I he type of group transferred or bond hydrolyzed for the lyases, it shows the nature of the group removed lor die isomerases. It indicates in more detail the nature ol the isonterizaiion and for the ligases. it shows the nature of the substance formed. Thus, un enzyme number, commonly indicated by the prefix EC. provides fairly deiailcd information about a specific enzyme. 

The second integer in an EC enzyme number indicates a sub-class for hydrolases, this second integer indicates the type of bond acted upon by the enzyme (Table 8.2). 

Figure 11.8 An example of the stochastic trajectory from Monte Carlo simulation according to the Gillespie algorithm for reaction system given in Equation (11.19) and corresponding master equation graph given in Figure 11.4. Here we set Ns = 100 and Nes = 0 at time zero and total enzyme number Ne = 10. (A) The fluctuating numbers of S and ES molecules as functions of time. (B) The stochastic trajectory in the phase space of (m, n).

The Gommission on Biochemical Nomenclature assigns enzyme numbers to 18 serine proteases in the 1972 edition of Enzyme Nomenclature (14). Seven are listed as having a trypsin-like specificity, i,e, their specific substrates have a positively charged lysine or arginine residue at Pi. Three are listed as having a chymotrypsin-like specificity, i.e., their specific substrates have residues of tryptophan, tyrosine, phenylalanine, or leucine at Pi, i,e, residues with bulky, hydrophobic side chains. Two enzymes have elastase-like specificities. They prefer a residue with... 

In brackets other name, sequence number (NCBI data base) or correct enzyme number.)... 

Sub-subclass (Nitrogenous group or acceptor) Enzyme number within sub-subclass —---------... 

The systematic name of an enzyme consists of two parts, the first originating from the equation, the second from the type of reaction catalyzed. In addition, according to the recommendations of the International Union of Pure and Applied Chemistry and the International Union of Biochemistry (1973), each enzyme bears a number from the international EC (Enzyme Classification) system, which reflects the main class, the subclass, and the subgroup. The number is completed by a special enzyme number. Thus, for example the EC number 1.1.3.4 of the enzyme with the trivial name glucose oxidase results from the following ... 

Enzymes Number of Substrates Overall Contribution to Drug Metabolism... 

The conserved active-site residues, His-48 and Asp-99 (pancreatic enzyme numbering), provide the catalytic dyad and, with the availability of the crystal structure of the pancreatic enzyme, have been shown to produce the proton-relay mechanism (Fig. 5) [17]. In this mechanism, a water molecule acts instead of the serine found in the classical protease/lipase catalytic triad mechanisms. More recently, an alternative mechanism of catalysis has been proposed that involves two water molecules (W5 and W6) seen at the active site of the crystal structure (Fig. 6). In this mechanism, proposed by Jain (J. Rogers,... 

Fig. 55. Reaction scheme of superoxide dismutation following the bovine enzyme numbering. The first O2 molecule binds to Cu(II) and is stabilized by the H bond to Arg-141. A second superoxide molecule then approaches the active site and, by an outer-sphere electron transfer via the Cu-bound first O2 molecule, reduces the copper to Cud) 44) (step III). Alternatively, O2" directly reduces superoxide to peroxide 336) (step IV), leaving as dioxygen. Note that the Cu(I)-superoxide and Cu(II)-peroxide complexes are resonant forms of the same molecular arrangement. The newly formed peroxide is protonated by Arg-141 and leaves as HO2. Arg-141 receives a proton from the solvent, restoring the active enz5Tne (I). These reaction proposals do not require the breaking and reforming of the Cu-His-61 bridge.

FIGURE 9.1 Simplified overview of lipid and lipoprotein metabolism with some key enzymes numbered (1) cholesteryl ester transfer protein (CETP), (2) hepatic triglyceride lipase, (3) lecithin cholesterol acyl transferase (LCAT), and (4) lipoprotein lipase. 

Family of enzymes Number of molecules of water fixed by a mol of albumin Grams of water fixed by 100 grams of albumin... 

The membrane-bound ATP(synth)ase affinity (Michaelis constant K ) for its substrates was found quite variable for ADP, from less than T yM (1) to almost 200 yM (2). In fact, this was predictable (3), inasmuch as the chemiosmotic mechanism of phosphorylation makes that, as soon as ADP is added, the proton channels open, the proton gradient A]5f + lowers, and consequently the catalytic constant and/or the enzyme number, because of their AvL+-dependent activation (4), decrease. That is, is not constant in the kinetic determination of K. ... 

NOTE 1 Enzyme names and enzyme numbers are taken from Enzyme Nomenclature, Recommendations (1978) of the Nomenclature Committee of the International Union of Biochemistry Academic Press, New York. With few exceptions, the recommended names are listed first in Section 34, followed by Other Names or synonyms in a set of brackets, and/or finally followed by the official enzyme numbers in a set of parentheses.]... 

Sample Enzymic activity (% remaining) 32pa (moles reagent/ mole enzyme) (moles reagent/ mole enzyme ) Number of residues of car-boxy-methyl cysteine Number of sulfhydryl groups modified... 

Figure 1. Lysosomal Digestive Pathways for Glycosaminoglycans. Each structure represents a type of repeating unit in the particular polysaccharide. Enzyme names with corresponding numbers are given in Table 2. A slash between two enzyme numbers indicates either reaction can precede the other.

RELAY/ENZYME NUMBER OF RELAYS PER ENZYME MOLECULE ACTIVITY OF MODIFIED ENZYME ACTIVITY OF NATIVE ENZYME... 

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