Table 5 Distance between catalytic amino acids (His239 for G6PDH, Lys183 for 6PGDH), and the amino acids detected as modified species, and their respective solvent exposures, are presented.

From: Implications of differential peroxyl radical-induced inactivation of glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase for the pentose phosphate pathway

G6PDH

6PGDH

Residue

Distance to His239 (Å)

ASA index

Residue

Distance to Lys183 (Å)

ASA index

Met

Met

M70

25.3

0.138

M11

19.1

0.005

M105

32.4

0.424

M14

8.8

0.240

M119

22.4

0.197

M73

9.9

0.066

M235

4.7

0.028

M141

6.1

0.000

M246

12.0

0.000

M184

10.6

0.017

M249

17.6

0.003

M194

11.5

0.002

M429

22.0

0.014

Trp

M458

29.3

0.852

W222

24.8

0.024

Trp

W265

9.7

0.174

W53

30.0

0.831

W349

15.6

0.034

W79

32.2

0.157

Tyr

W201

20.6

0.005

Y149

15.9

0.070

W223

20.9

0.504

Y230

12.0

0.161

W326

27.6

0.652

W328

21.1

0.007

W364

37.1

0.556

W446

11.2

0.051

W448

13.9

0.013

W456

21.4

0.082

  1. The amino acids with modifications > 50% (see Fig. 7) believed to be involved in the loss of activity elicited by ROO· are indicated in Bold text. These residues were selected on the basis of their proximity to His239 (G6PDH) or Lys183 (6PGDH) and/or their solvent exposure (determined by ASA index, 0–1). Analyses were carried out using the protein sequences reported in UniProt database entries P0AC53 and P00350, for G6PDH and 6PGDH, respectively. The sidechains of the catalytic site His239 (imidazole ring) and Lys183 (nitrogen atom) were used to calculate the distance to the Met (sulfur atom) and Trp (indole ring) residues of the oxidized residues.
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