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Table 3 Pairwise parameters for candidate alkane hydroxylases in two conserved pfam domains, p450 and Pry_redox_3

From: Alkane hydroxylase genes in psychrophile genomes and the potential for cold active catalysis

pfam domain

Protein region

Protein parameter

Total number of comparisons1

Cases where psychrophile was higher

p450

Whole

Isoelectric point

9

0

p450

Whole

Asparagine

9

8

p450

Whole

Arginine

9

0

p450

Whole

Threonine

9

8

p450

Whole

Valine

9

9

p450

Coil

Isoleucine

9

8

p450

Coil

Aspargine

9

9

p450

Coil

Valine

9

9

p450

β-sheet

Flexibility

9

8

p450

β-sheet

Isoelectric point

9

8

p450

β-sheet

Alanine

9

8

p450

β-sheet

Glycine

9

9

p450

β-sheet

Isoleucine

9

1

p450

β-sheet

Proline

9

9

p450

α-helix

Flexibility

9

8

p450

α-helix

Aspartic acid

9

9

p450

α-helix

Isoleucine

9

0

p450

α-helix

Arginine

9

0

Pyr_redox_3

Whole

Cysteine

11

10

Pyr_redox_3

Whole

Glutamic acid

11

0

Pyr_redox_3

Whole

Valine

11

10

Pyr_redox_3

Coil

Aspartic acid

11

10

Pyr_redox_3

Coil

Glycine

11

1

Pyr_redox_3

β-sheet

GRAVY

11

10

Pyr_redox_3

β-sheet

Cysteine

11

11

Pyr_redox_3

α-helix

Alanine

11

10

Pyr_redox_3

α-helix

Glutamic acid

11

0

Pyr_redox_3

α-helix

Asparagine

11

1

  1. Amino acids in the parameter column refer to amino acid content.
  2. 1All psychrophile candidate alkane hydroxylases within a pfam were compared with all mesophile candidate alkane hydroxylases in that pfam for a given protein secondary structure (region), protein parameter, and taxonomic pair, where the total number of comparisons possible was 9 or 11 (see Table 2).