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Introduction to Enzyme and Coenzyme Chemistry - E-Library Home

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162 Chapter 7<br />

Figure 7.6 Active site of Escherichia coli fruc<strong>to</strong>se-1,6-bisphosphate aldolase (PDB Wle 1B57), a class<br />

II aldolase. Bound substrate analogue phosphoglycolohydroxamate <strong>and</strong> Zn 2þ cofac<strong>to</strong>r shown in<br />

black. Catalytic residues Asp-109 (bot<strong>to</strong>m) <strong>and</strong> Glu-182 (<strong>to</strong>p left), <strong>and</strong> Zn 2þ lig<strong>and</strong>s shown in red.<br />

Glu 182<br />

O −<br />

O<br />

H S<br />

H R<br />

OPO 3<br />

2−<br />

O<br />

H<br />

O<br />

2+<br />

Zn<br />

NHis<br />

NHis<br />

NHis<br />

2− O 3 PO<br />

O<br />

Asp 109<br />

O<br />

H<br />

H<br />

OH<br />

O<br />

H<br />

H<br />

OPO 3<br />

2−<br />

O<br />

H<br />

O −<br />

2+<br />

Zn<br />

NHis<br />

NHis<br />

NHis<br />

2− O3 PO<br />

H<br />

OH<br />

OPO 3<br />

2−<br />

HO<br />

O −<br />

O<br />

H<br />

H<br />

O<br />

H<br />

O<br />

2+<br />

Zn<br />

NHis<br />

NHis<br />

NHis<br />

Asp 109<br />

Figure 7.7 Mechanism for Eschericha coli class II fruc<strong>to</strong>se-1,6-biphosphate aldolase.

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