11.相关中文翻译：

http://atp.life.nctu.edu.tw/~biocenter/sections.php?op=viewarticle&artid=74

allosteric enzyme 异位调节酵素(变构酶)

中文： 異位調節酵素
說明：異位調節酵素多半是由2個以上的次單位所組成，包括具有酵素作用，可與效應物結合的催化次單位(catalytic subunit)及可與效應物結合的調節次單位(regulatory subunit)。當異位效應物與調節次單位結合時，其構造上會發生變化，並影響催化次單位，使得受質與酵素間的結合力變弱。
定義：酵素分子與其他物質(如效應物effector)結合時，其結合位置並非酵素分子和受質(substrate)的結合部位，結果在酵素的分子結構上發生變化，因而酵素活性會被促進或抑制。這種現象稱為異位效應(allosteric effect)，具有這種效應的酵素稱為異位調節酵素。異位效應是生物體中代謝調節的重要機制之一。

active site 活性基
在酶(enzyme)分子表面的裂縫，可与受质(substrate)分子表面特定区域結合并活化之。

feedback inhibition 回馈抑制
当体內某些物质或活动增加时，會回转抑制使其增加的主要因素或过程的一种生物控制的机制。

Other interpretations:

allosteric

（biochemistry, chemistry） Of a binding site in a protein, usually an enzyme.

The catalytic function of an enzyme may be modified by interaction with small molecules, not only at the active site, but also at a spatially distinct (allosteric) site of different specificity.

Of a protein, a protein possessing such a site. An allosteric effector is a molecule bound at such a site that increases or decreases the activity of the enzyme.

active site:  A specific region of an enzyme where a substrate binds and catalysis takes place (binding site).

中国教材中的术语：

变构部位 allosteric site
变构调节 allosteric regulation
变构激活剂 allosteric activator
变构酶 allosteric enzyme
变构效应 allosteric effect
变构效应剂 allosteric effector
变构抑制剂 allosteric inhibitor 

4. allosteric control

        http://www.britannica.com/eb/article-9005828

      in enzymology, inhibition or activation of an enzyme by a small regulatory molecule that interacts at a site (allosteric site) other than the active site (at which catalytic activity occurs). The interaction changes the shape of the enzyme so as to affect the formation at the active site of the usual complex between the enzyme and its substrate (the compound upon which it acts to form a product). As a result, the ability of the enzyme to catalyze a reaction is modified. This is the basis of the so-called induced-fit theory, which states that the binding of a substrate or some other molecule to an enzyme causes a change in the shape of the enzyme so as to enhance or inhibit its activity.

The regulatory molecule may be a product of a synthetic pathway and inhibit an enzyme in that pathway (see feedback inhibition), thereby preventing the further formation of itself. Other molecules act as activators; i.e., they interact with an enzyme so as to enhance the binding of the substrate to the enzyme, thus enhancing catalytic activity. The enzyme adenyl cyclase, itself activated by the hormone adrenaline (epinephrine), which is released when a mammal requires energy, catalyzes a reaction that results in the formation of the compound cyclic adenosine monophosphate (cyclic AMP). Cyclic AMP, in turn, activates enzymes that metabolize carbohydrates for energy production. A combination of allosteric activation and inhibition thus provides a way by which the cell can rapidly regulate needed substances.

5. feedback inhibition

   http://www.britannica.com/eb/article-9033914/feedback-inhibition

      in enzymology, suppression of the activity of an enzyme, participating in a sequence of reactions by which a substance is synthesized, by a product of that sequence. When the product accumulates in a cell beyond an optimal amount, its production is decreased by inhibition of an enzyme involved in its synthesis. After the product has been utilized or broken down and its concentration thus decreased, the inhibition is relaxed, and the formation of the product resumes. Such enzymes, whose ability to catalyze a reaction depends upon molecules other than their substrates (the ones upon which they act to form a product), are said to be under allosteric control. Feedback inhibition is a mechanism by which the concentration of certain cell constituents is limited.

6. The induced-fit theory (protein)

     http://www.britannica.com/eb/article-72596/protein#593882.hook

      The key–lock hypothesis (see above The nature of enzyme-catalyzed reactions) does not fully account for enzymatic action; i.e., certain properties of enzymes cannot be accounted for by the simple relationship between enzyme and substrate proposed by the key–lock hypothesis. A theory called the induced-fit theory retains the key–lock idea of a fit of the substrate at the active site but postulates in addition that the substrate must do more than simply fit into the already preformed shape of an active site. Rather, the theory states, the binding of the substrate to the enzyme must cause a change in the shape of the enzyme that results in the proper alignment of the catalytic groups on its surface. This concept has been likened to the fit of a hand in a glove, the hand (substrate) inducing a change in the shape of the glove (enzyme). Although some enzymes appear to function according to the older key–lock hypothesis, most apparently function according to the induced-fit theory.
       During step 1 in Figure 10, which illustrates the induced-fit theory, the substrate approaches the enzyme surface and induces a change in its shape that results in the correct alignment of the catalytic groups (indicated by triangles A and B). In the case of the digestive enzyme carboxypeptidase, the binding of the substrate causes a tyrosine molecule at the active site to move by as much as 15 angstroms. Circles C and D in the figure represent substrate-binding groups on the enzyme that are essential for catalytic activity. During step 2 the catalytic groups at the active site react with the substrate to form products. The products separate from the enzyme surface during step 3, and the enzyme is able to repeat the sequence.
         Nonsubstrate molecules that are too bulky (Figure 10D) or too small (Figure 10E) alter the shape of the enzyme so that a misalignment of catalytic groups A and B occurs; such molecules are not able to react even if they are attracted to the active site.
       The induced-fit theory explains a number of anomalous properties of enzymes; for example, “noncompetitive inhibition” (Figure 10F), in which a compound inhibits the reaction of an enzyme but does not prevent the binding of the substrate. In this case, the inhibitor compound I attracts the binding group C so that the catalytic group B is too far away from the substrate to react. The site at which the inhibitor binds to the enzyme is not the active site and is called an allosteric site. The inhibitor changes the shape of the active site to prevent catalysis without preventing binding of the substrate.
       Figure 10G shows the effect of an inhibitor (¢l), which distorts the active site by affecting the essential binding group D; as a result, the enzyme can no longer attract the substrate. In Figure 10H, a so-called activator molecule, X, affects the active site so that a nonsubstrate molecule is properly aligned and hence can react with the enzyme; X is called an allosteric activator of the reaction. Such activators can affect both binding and catalytic groups at the active site.
     Enzyme flexibility is extremely important because it provides a mechanism for regulating enzymatic activity. As shown in Figure 10F and G, the orientation at the active site can be disrupted by the binding of an inhibitor at a site other than the active site. Moreover, the enzyme can be activated by molecules that induce a proper alignment of the active site for a substrate that alone cannot induce this alignment (Figure 10H).

     As mentioned above, the sites that bind inhibitors and activators are called allosteric sites to distinguish them from active sites. Allosteric sites are in fact regulatory sites able to activate or inhibit enzymatic activity by influencing the shape of the enzyme. When the activator or inhibitor dissociates from the enzyme, it returns to its normal shape. Thus, the flexibility of the protein structure allows the operation of a simple, reversible control system similar to a thermostat.： 

1.allosteric.

    Pronunciation: "a-lo-'ster-ik; ( adjective)
    Etymology: all- + steric
    of, relating to, undergoing, or being a change in the shape and activity of a protein (as an enzyme) that results from combination with another substance at a point other than the chemically active site

2. allosteric regulation

（http://en.wikipedia.org/wiki/Allosteric_regulation）

      In biochemistry, allosteric regulation is the regulation of an enzyme or protein by binding an effector molecule at the protein's allosteric site (that is, a site other than the protein's active site). Effectors that enhance the protein's activity are referred to as allosteric activators, whereas those that decrease the protein's activity are called allosteric inhibitors. The term allostery comes from the Greek allos, "other," and stereos, "space," referring to the regulatory site of an allosteric protein's being separate from its active site. Allosteric regulation is a natural example of feedback control

3. effector

     (http://en.wikipedia.org/wiki/Effector_%28biology%29)

       An effector is a molecule (originally referring to small molecules but now encompassing any regulatory molecule, includes proteins) that binds to a protein and thereby alters the activity of that protein. A modulator molecule binds to a regulatory site during allosteric modulation and allosterically modulates the shape of the protein.

    Types of effectors：

      3-1. Enzyme activators are molecules that bind to enzymes and increase their activity. These molecules are often involved in the allosteric regulation of enzymes in the control of metabolism. An example of an enzyme activator working in this way is fructose 2,6-bisphosphate, which activates phosphofructokinase 1 and increases the rate of glycolysis in response to the hormone glucagon.

      3-2. Enzyme inhibitors are molecules that bind to enzymes and decrease their activity. Since blocking an enzyme's activity can kill a pathogen or correct a metabolic imbalance, many drugs are enzyme inhibitors. They are also used as herbicides and pesticides. Not all molecules that bind to enzymes are inhibitors; enzyme activators bind to enzymes and increase their enzymatic activity.

       The binding of an inhibitor can stop a substrate from entering the enzyme's active site and/or hinder the enzyme from catalysing its reaction. Inhibitor binding is either reversible or irreversible. Irreversible inhibitors usually react with the enzyme and change it chemically. These inhibitors modify key amino acid residues needed for enzymatic activity. In contrast, reversible inhibitors bind non-covalently and different types of inhibition are produced depending on whether these inhibitors bind the enzyme, the enzyme-substrate complex, or both.

       Many drug molecules are enzyme inhibitors, so their discovery and improvement is an active area of research in biochemistry and pharmacology. A medicinal enzyme inhibitor is often judged by its specificity (its lack of binding to other proteins) and its potency (its dissociation constant, which indicates the concentration needed to inhibit the enzyme). A high specificity and potency ensure that a drug will have few side effects and thus low toxicity.         Enzyme inhibitors also occur naturally and are involved in the regulation of metabolism. For example, enzymes in a metabolic pathway can be inhibited by downstream products. This type of negative feedback slows flux through a pathway when the products begin to build up and is an important way to maintain homeostasis in a cell. Other cellular enzyme inhibitors are proteins that specifically bind to and inhibit an enzyme target. This can help control enzymes that may be damaging to a cell, such as proteases or nucleases; a well-characterised example is the ribonuclease inhibitor, which binds to ribonucleases in one of the tightest known protein–protein interactions.^[1] Natural enzyme inhibitors can also be poisons and are used as defenses against predators or as ways of killing prey. 

儿子在我们不在家的日子里长大

My son grows up, while with less our accompanying......

跟儿子的交流，每每彼此很开心。尤其是我，得到了太多的来自儿子的鼓励，他让我变得坚强，让我忘记自己的年龄…….每听到他的声音，我觉得我很Young!

今天下午刚刚在法领馆renew了schengen visa, 便接到了老公先生发来的短信，他又出发了！儿子又是一个人在家里！我放心不下。老公先生接着转发来一条短信，是儿子的。觉得挺有意思，这是一段对他对友情的理解：

他们几个和我在祖国的东西南北，各一方。夏天保送了，于达到了山东大学，王烨到了南昌，还有不少同学到了上海。他们还说很想我。说要在我高考后在济南依聚一聚。感动啊！什么是真正的友情，我算是体会到了！原来我也是一个幸福的人，在初中的感情还能够跨越时间和空间的界限。在此刻，友情在温暖我的心，我还有什么可以奢求的呢？

看到这一段，我完全明白儿子此时的心情…………

接着，拨通了家里的电话，是儿子那略带男子汉磁性的声音.....

儿子：“Hi, 妈妈！”

       “妈妈读到你的短信，真是好羡慕你！”

儿子：“羡慕我什么？”

“你那么年轻！有那么美丽的青春！可以做你想做的很多事情！”

儿子：“是啊，可是我现在还是要好好准备！”

“没问题的！我绝对相信你！妈妈的条件就不如你了，你是朝阳，妈妈已近落日黄昏了！我只好倍加努力了！”

儿子：“不能这么说吗！真么是黄昏呢？ 至少是午后的烈日！”

“哈…….

儿子“我正在考虑怎么把生日礼物送到你手里。我在联系瑞士的邮政……我想还是玫瑰比较好..”

“哦！ 谢谢你，总是你第一个想着我！”

儿子“不，还有我爸爸也想着你！其实，我姥姥最想着你！”

    “我也很想你们！把想念保存起来吧！去做更值得做的的事情！生日那天，我不在日内瓦，我用旅行作为大家对我的生日的祝贺”。

儿子：“那好，我提前祝你生日快乐！”

……………..

我算了一下，在儿子读书的近12年中，我花了近七年，离开他，去圆我的读书梦……没想到，没完没了…….

小学的时候，儿子的作文凡是得高分的，都是写的跟妈妈有关的故事。老师说，你的儿子是在想妈妈的日子里长大的…..

上初中的时候，他的语文老师很惊讶，一个捣蛋男孩怎么会用有限的文字把妈妈描绘的那么细腻感人……

到了高中，他开始用新的方式表达对我们三口之家中唯一女士的关爱，送小礼物、骑自行车带我兜风、一起散步、一起买菜……每当我下班回家，只要他先到家，就开门，赶紧接下我身上背的、手里拎的东西……

他是一个很会“算计”的男生，每月不多的零花前被他管理得很好。我来瑞士的时候，他用积攒下来的零花钱为我“换来”一个“安睡小天使”，别说，那“小天使”的模样还真是很像我！我带“她”来到了瑞士，现在她就在我的床头柜上。有她的陪伴，我的失眠毛病好了许多…….

其实，最快乐的，还是我们三人一起外出，在他们两条大汉之间，“架着”我这个被他俩称作的“小矮人”……

然而，我们三人到齐的时候并不多。每当我或先生离家多日，再见到儿子的时候，总是发现：他怎么又变了？

儿子是在我们不在家的时候长大的...... 

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