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Table 2 Sequence and structure comparison of the eight-residue loops of family 11 xylanases

From: Improvement of alkalophilicity of an alkaline xylanase Xyn11A-LC from Bacillus sp. SN5 by random mutation and Glu135 saturation mutagenesis

Enzyme abbreviation

Source

PDB code

Eight-residue loop sequence

Salt-bridge in the eight-residue loop

Optimum pH

XynJ (∆XBD)

Bacillus sp. 41M-1

2DCK

QPSIKGTA

Lys135- Glu55

9 [17]

Xyl C

alkalophilic Bacillus (NCL 87-6-10)

2F6B

QPSIKGIA

Lys136-Glu56

8 [35]

BadX

Bacillus agaradhaerens AC13

1H4G

QPSIKGIA

Lys136- Glu56

8 [36]

Xyn11X

Bacillus subtilis B230

1IGO

QPSIIGIA

NA

8 [37]

Xyn11A-LC

Bacillus sp SN5

4IXL

QPSIEGTA

NA

7.5 [18]

XynA

Bacillus subtilis 168(1A1)

1XXN

APSIDGDR

NA

6–6.5 [38]

Xyl1

Streptomyces sp. S38

1HIX

APSVEGTK

NA

6 [39]

Bcx

Bacillus circulans

1XNB

APSIDGDR

NA

5.7 [40]

Xyn2

Hypocrea jecorina RUT-C30

1XYO

QPSIIGTA

NA

5.3 [21]

XYNI

Trichoderma reesei

1XYN

EPSIQGTA

NA

3.5 [41]

XYL1

Scytalidium acidophilum

3M4F

EPSITGTS

NA

3.2 [42]

XynA

Aspergillus niger CBS 513.88

1UKR

EPSITGTS

NA

3 [43]

XynC

Aspergillus kawachii

1BK1

EPSITGTS

NA

2 [44]

  1. The key residues involved in the pH adaptation of enzymes are in bold and underlined