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Histidine production

The selective pressure calculated above was generated merely by the capability of the cell to adjust its histidine production to varying growth rates. Had histidine been available in the medium, an even greater amount of metabolic energy would have been uselessly spent. Conversely, it is a trivial but often overlooked deduction that active transport systems for exogenously available biosynthetic products can be of benefit only when the intracellular biosynthesis of those products is subject to control. [Pg.359]

This review has pointed out that the major control element in histidine production is feedback inhibition of the first enzyme of the pathway. However, most of the work on regulation of the operon has been devoted to repression control. This is partly because less is known about... [Pg.382]

A base, formed by the bacterial degradation of histidine, and present in ergot and in many animal tissues, where it is liberated in response to injury and to antigen-antibody reactions. If injected it causes a condition of shock with dilatation of many blood vessels, loss of plasma from the capillaries to the tissues and a rapid fall in blood pressure. It is normally prepared from protein degradation products. [Pg.204]

CfiHqNaO . M.p. 277 C. The naturally occurring substance is laevorotatory. Histidine is one of the basic amino-acids occurring in the hydrolysis products of proteins, and particularly of the basic proteins, the protamines and histones. It is an essential constituent of the food of animals. [Pg.205]

Step 3 of Figure 29.3 Alcohol Oxidation The /3-hydroxyacyl CoA from step 2 is oxidized to a /3-ketoacyl CoA in a reaction catalyzed by one of a family of L-3-hydroxyacyl-CoA dehydrogenases, which differ in substrate specificity according to the chain length of the acyl group. As in the oxidation of sn-glycerol 3-phosphate to dihydroxyacetone phosphate mentioned at the end of Section 29.2, this alcohol oxidation requires NAD+ as a coenzyme and yields reduced NADH/H+ as by-product. Deprotonation of the hydroxyl group is carried out by a histidine residue at the active site. [Pg.1136]

The crude product is dissolved in five times its weight of water, and after clearing with a little Norite the solution is diluted with one and one-half volumes of 95 per cent alcohol. The product separates in well-formed, snow-white crystals, and after standing for several days in an ice chest is collected with suction on a Buchner funnel. The yield of purified histidine monohydrochloride is 75-80 g. (Note 5). The compound melts at 251-2520, with decomposition. The amino acid is not race-mized by the procedure employed, and shows the characteristic optical activity, [a]n6° = +8.00, in the presence of three moles of... [Pg.44]

Hiroshima, 721 histidine, 443, 774 hole, 195 homeostasis, 386 HOMO, 126, 580 homogeneous alloy, 202 homogeneous catalyst, 565 homogeneous equilibria, 362 homogeneous mixture, F53 homolytic dissociation, 80 homonuclear diatomic molecule, 103 Hooke s law, 92 hormone, 670 horsepower, A4, 791 hour, A4 HPLC, 354 HRF products, 723 HTSC, 192 Humphreys series, 51 Hund, F 35 Hund s rule, 35, 37 Hurricane Rita, 144 hyaluronic acid, 344 hybrid orbital, 109 hybridization bond angle, 131 molecular shape, 111 hydrangea color, 463 hydrate, F32 hydrate isomer, 676 hydration, 178 hydrazine, 627... [Pg.1033]

The mechanism for the lipase-catalyzed reaction of an acid derivative with a nucleophile (alcohol, amine, or thiol) is known as a serine hydrolase mechanism (Scheme 7.2). The active site of the enzyme is constituted by a catalytic triad (serine, aspartic, and histidine residues). The serine residue accepts the acyl group of the ester, leading to an acyl-enzyme activated intermediate. This acyl-enzyme intermediate reacts with the nucleophile, an amine or ammonia in this case, to yield the final amide product and leading to the free biocatalyst, which can enter again into the catalytic cycle. A histidine residue, activated by an aspartate side chain, is responsible for the proton transference necessary for the catalysis. Another important factor is that the oxyanion hole, formed by different residues, is able to stabilize the negatively charged oxygen present in both the transition state and the tetrahedral intermediate. [Pg.172]


See other pages where Histidine production is mentioned: [Pg.115]    [Pg.220]    [Pg.134]    [Pg.219]    [Pg.351]    [Pg.351]    [Pg.359]    [Pg.115]    [Pg.220]    [Pg.134]    [Pg.219]    [Pg.351]    [Pg.351]    [Pg.359]    [Pg.409]    [Pg.289]    [Pg.290]    [Pg.322]    [Pg.47]    [Pg.628]    [Pg.1043]    [Pg.1149]    [Pg.18]    [Pg.23]    [Pg.692]    [Pg.853]    [Pg.391]    [Pg.52]    [Pg.537]    [Pg.295]    [Pg.415]    [Pg.416]    [Pg.230]    [Pg.228]    [Pg.853]    [Pg.40]    [Pg.16]    [Pg.336]    [Pg.359]    [Pg.113]    [Pg.47]    [Pg.29]    [Pg.157]    [Pg.49]    [Pg.272]    [Pg.1189]    [Pg.166]    [Pg.66]    [Pg.171]    [Pg.266]   
See also in sourсe #XX -- [ Pg.80 ]




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Histidine decarboxylated product

Histidine endogenous production

Histidine metabolism, products

Histidine natural products

Secondary Products Synthesized from L-Histidine

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