- Teks
- Sejarah
7.6.2 CoenzymesWe shall continue wi
7.6.2 Coenzymes
We shall continue with the role of NAD
+
as coenzyme for alcohol dehydrogenase. Figure 26 is a schematic diagram of NAD
bound in the active site of yeast alcohol dehydrogenase, with the adenine ribose phosphate (ADPR) moiety bound at the ADPR
binding site. The nicotinamide moiety, the functional part of NAD
in accepting H from the ethanol , is bound into the
lipophobic binding site. Zn
2+
+
, a cation cofactor, is required also; it is shown liganded to three amino acid side chains on the
protein and coordinately bound to the O of the OH group of ethanol. A tetrahedral intermediate is formed in step 2 followed by
transfer of the H from ethanol to from NADH. The turnover number is about 10
moles of substrate converted to product
permole enzyme per second. Therefore, the recycle time is about 1 msec.
The primary role of the alcohol dehydrogenase is as a specific template, binding ethanol, NAD
3
+
, and Zn
stereospecifically at
the active site. As discussed in Section 7.5.7, that is a very significant role, accounting for ~10
rate enhancement. It must also
be remembered that the enzyme provides stereospsecific treatment of the substrate. Even though ethanol does not have an
asymmetric carbon atom, the enzyme always recognizes ethanol as being asymmetric because of the three-point attachment in
the transition state (Fig. 26). The protein also provides the environment, often hydrophobic, in which the reaction takes place.
15
2+
+
We shall continue with the role of NAD
+
as coenzyme for alcohol dehydrogenase. Figure 26 is a schematic diagram of NAD
bound in the active site of yeast alcohol dehydrogenase, with the adenine ribose phosphate (ADPR) moiety bound at the ADPR
binding site. The nicotinamide moiety, the functional part of NAD
in accepting H from the ethanol , is bound into the
lipophobic binding site. Zn
2+
+
, a cation cofactor, is required also; it is shown liganded to three amino acid side chains on the
protein and coordinately bound to the O of the OH group of ethanol. A tetrahedral intermediate is formed in step 2 followed by
transfer of the H from ethanol to from NADH. The turnover number is about 10
moles of substrate converted to product
permole enzyme per second. Therefore, the recycle time is about 1 msec.
The primary role of the alcohol dehydrogenase is as a specific template, binding ethanol, NAD
3
+
, and Zn
stereospecifically at
the active site. As discussed in Section 7.5.7, that is a very significant role, accounting for ~10
rate enhancement. It must also
be remembered that the enzyme provides stereospsecific treatment of the substrate. Even though ethanol does not have an
asymmetric carbon atom, the enzyme always recognizes ethanol as being asymmetric because of the three-point attachment in
the transition state (Fig. 26). The protein also provides the environment, often hydrophobic, in which the reaction takes place.
15
2+
+
0/5000
7.6.2 Coenzymes
We shall continue with the role of NAD
+
as coenzyme for alcohol dehydrogenase. Figure 26 is a schematic diagram of NAD
bound in the active site of yeast alcohol dehydrogenase, with the adenine ribose phosphate (ADPR) moiety bound at the ADPR
binding site. The nicotinamide moiety, the functional part of NAD
in accepting H from the ethanol , is bound into the
lipophobic binding site. Zn
2+
+
, a cation cofactor, is required also; it is shown liganded to three amino acid side chains on the
protein and coordinately bound to the O of the OH group of ethanol. A tetrahedral intermediate is formed in step 2 followed by
transfer of the H from ethanol to from NADH. The turnover number is about 10
moles of substrate converted to product
permole enzyme per second. Therefore, the recycle time is about 1 msec.
The primary role of the alcohol dehydrogenase is as a specific template, binding ethanol, NAD
3
+
, and Zn
stereospecifically at
the active site. As discussed in Section 7.5.7, that is a very significant role, accounting for ~10
rate enhancement. It must also
be remembered that the enzyme provides stereospsecific treatment of the substrate. Even though ethanol does not have an
asymmetric carbon atom, the enzyme always recognizes ethanol as being asymmetric because of the three-point attachment in
the transition state (Fig. 26). The protein also provides the environment, often hydrophobic, in which the reaction takes place.
15
2+
+
We shall continue with the role of NAD
+
as coenzyme for alcohol dehydrogenase. Figure 26 is a schematic diagram of NAD
bound in the active site of yeast alcohol dehydrogenase, with the adenine ribose phosphate (ADPR) moiety bound at the ADPR
binding site. The nicotinamide moiety, the functional part of NAD
in accepting H from the ethanol , is bound into the
lipophobic binding site. Zn
2+
+
, a cation cofactor, is required also; it is shown liganded to three amino acid side chains on the
protein and coordinately bound to the O of the OH group of ethanol. A tetrahedral intermediate is formed in step 2 followed by
transfer of the H from ethanol to from NADH. The turnover number is about 10
moles of substrate converted to product
permole enzyme per second. Therefore, the recycle time is about 1 msec.
The primary role of the alcohol dehydrogenase is as a specific template, binding ethanol, NAD
3
+
, and Zn
stereospecifically at
the active site. As discussed in Section 7.5.7, that is a very significant role, accounting for ~10
rate enhancement. It must also
be remembered that the enzyme provides stereospsecific treatment of the substrate. Even though ethanol does not have an
asymmetric carbon atom, the enzyme always recognizes ethanol as being asymmetric because of the three-point attachment in
the transition state (Fig. 26). The protein also provides the environment, often hydrophobic, in which the reaction takes place.
15
2+
+
Sedang diterjemahkan, harap tunggu..
7.6.2 Koenzim
Kita akan melanjutkan peran NAD
+
sebagai koenzim untuk alkohol dehidrogenase. Gambar 26 adalah diagram skematik dari NAD
terikat pada sisi aktif dari dehidrogenase ragi alkohol, dengan adenin ribose fosfat (ADPR) bagian terikat di ADPR
situs mengikat. Separoh nicotinamide, bagian fungsional dari NAD
dalam menerima H dari etanol, terikat ke dalam
situs pengikatan lipofob. Zn
2+
+
, kofaktor kation, diperlukan juga; yang terlihat liganded tiga amino rantai samping asam pada
protein dan terkoordinasi terikat pada O dari gugus OH etanol. Sebuah tetrahedral menengah dibentuk pada langkah 2 diikuti oleh
transfer H dari etanol ke dari NADH. Jumlah omset sekitar 10
mol substrat dikonversi ke produk
enzim permole per detik. Oleh karena itu, waktu recycle sekitar 1 msec.
Peran utama dari dehidrogenase alkohol sebagai template tertentu, etanol mengikat, NAD
3
+
, dan Zn
stereospecifically di
situs aktif. Sebagaimana dibahas dalam Bagian 7.5.7, yang merupakan peran yang sangat signifikan, akuntansi untuk ~ 10
peningkatan tingkat. Hal ini juga harus
diingat bahwa enzim menyediakan pengobatan stereospsecific substrat. Meskipun etanol tidak memiliki
atom karbon asimetrik, enzim selalu mengakui etanol sebagai asimetris karena tiga titik lampiran dalam
keadaan transisi (Gambar. 26). Protein juga menyediakan lingkungan, sering hidrofobik, di mana reaksi berlangsung.
15
2+
+
Kita akan melanjutkan peran NAD
+
sebagai koenzim untuk alkohol dehidrogenase. Gambar 26 adalah diagram skematik dari NAD
terikat pada sisi aktif dari dehidrogenase ragi alkohol, dengan adenin ribose fosfat (ADPR) bagian terikat di ADPR
situs mengikat. Separoh nicotinamide, bagian fungsional dari NAD
dalam menerima H dari etanol, terikat ke dalam
situs pengikatan lipofob. Zn
2+
+
, kofaktor kation, diperlukan juga; yang terlihat liganded tiga amino rantai samping asam pada
protein dan terkoordinasi terikat pada O dari gugus OH etanol. Sebuah tetrahedral menengah dibentuk pada langkah 2 diikuti oleh
transfer H dari etanol ke dari NADH. Jumlah omset sekitar 10
mol substrat dikonversi ke produk
enzim permole per detik. Oleh karena itu, waktu recycle sekitar 1 msec.
Peran utama dari dehidrogenase alkohol sebagai template tertentu, etanol mengikat, NAD
3
+
, dan Zn
stereospecifically di
situs aktif. Sebagaimana dibahas dalam Bagian 7.5.7, yang merupakan peran yang sangat signifikan, akuntansi untuk ~ 10
peningkatan tingkat. Hal ini juga harus
diingat bahwa enzim menyediakan pengobatan stereospsecific substrat. Meskipun etanol tidak memiliki
atom karbon asimetrik, enzim selalu mengakui etanol sebagai asimetris karena tiga titik lampiran dalam
keadaan transisi (Gambar. 26). Protein juga menyediakan lingkungan, sering hidrofobik, di mana reaksi berlangsung.
15
2+
+
Sedang diterjemahkan, harap tunggu..
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- De partijen willen een overeenkomsten sl
- keep the spirit
