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Literature summary for 3.1.1.74 extracted from

  • Skamnioti, P.; Furlong, R.; Gurr, S.
    Evolutionary history of the ancient cutinase family in five filamentous Ascomycetes reveals differential gene duplications and losses and in Magnaporthe grisea shows evidence of sub- and neo-functionalization (2008), New Phytol., 180, 711-721.
    View publication on PubMed

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
30100
-
sequence analysis Aspergillus nidulans
36400
-
sequence analysis Fusarium graminearum
38700
-
sequence analysis Botrytis cinerea
39200
-
sequence analysis Neurospora crassa
41200
-
sequence analysis Pyricularia grisea

Organism

Organism UniProt Comment Textmining
Aspergillus nidulans
-
-
-
Botrytis cinerea
-
-
-
Fusarium graminearum
-
-
-
Neurospora crassa
-
-
-
no activity in Saccharomycotina
-
-
-
Pyricularia grisea
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information four cysteine residues pivotal to the formation of the two disulphide bridges and a highly conserved cut-1 motif (GYSQG) surrounding a cutinase active serine, but a less precise cut-2 motif, DxVCxG(ST)-(LIVMF)(3)-x(3)H, which carries the aspartate and histidine residues of the active site Aspergillus nidulans ?
-
?
additional information four cysteine residues pivotal to the formation of the two disulphide bridges and a highly conserved cut-1 motif (GYSQG) surrounding a cutinase active serine, but a less precise cut-2 motif, DxVCxG(ST)-(LIVMF)(3)-x(3)H, which carries the aspartate and histidine residues of the active site Neurospora crassa ?
-
?
additional information four cysteine residues pivotal to the formation of the two disulphide bridges and a highly conserved cut-1 motif (GYSQG) surrounding a cutinase active serine, but a less precise cut-2 motif, DxVCxG(ST)-(LIVMF)(3)-x(3)H, which carries the aspartate and histidine residues of the active site Fusarium graminearum ?
-
?
additional information four cysteine residues pivotal to the formation of the two disulphide bridges and a highly conserved cut-1 motif (GYSQG) surrounding a cutinase active serine, but a less precise cut-2 motif, DxVCxG(ST)-(LIVMF)(3)-x(3)H, which carries the aspartate and histidine residues of the active site Botrytis cinerea ?
-
?
additional information four cysteine residues pivotal to the formation of the two disulphide bridges and a highly conserved cut-1 motif (GYSQG) surrounding a cutinase active serine, but a less precise cut-2 motif, DxVCxG(ST)-(LIVMF)(3)-x(3)H, which carries the aspartate and histidine residues of the active site. Two exceptions: one cutinase gene is truncated at the 3' end immediately after the cut-1 motif owing to a gap in the genomic sequence, and one cutinase gene, which is truncated at the 3' end shortly before the cut-2 motif because of a repetitive sequence, making further prediction impossible Pyricularia grisea ?
-
?

Subunits

Subunits Comment Organism
? x * 38700, calculated from sequence Botrytis cinerea
? x * 30100, calculated from sequence Aspergillus nidulans
? x * 36400, calculated from sequence Fusarium graminearum
? x * 39200, calculated from sequence Neurospora crassa
? x * 41200, calculated from sequence Pyricularia grisea

Synonyms

Synonyms Comment Organism
cutinase
-
Aspergillus nidulans
cutinase
-
Neurospora crassa
cutinase
-
Pyricularia grisea
cutinase
-
Fusarium graminearum
cutinase
-
Botrytis cinerea
cutinase
-
no activity in Saccharomycotina

Expression

Organism Comment Expression
Pyricularia grisea cutinase genes show four differential expression patterns, indicating regulatory sub- and neo-functionalization additional information

General Information

General Information Comment Organism
physiological function contains four cutinase genes, which may result from its low repetitive content and mild form of repeat induced point mutation Aspergillus nidulans
physiological function contains three cutinases, which show less than 80% sequence identity, indicating that they are duplicated and diverged before the emergence of the active repeat induced point mutation defence mechanism, and have been retained in the genome by virtue of their varying regulatory or functional diversity Neurospora crassa
physiological function the organism contains 11 cutinases, despite the 3-4% repetitive DNA content and the repeat induced point mutation-based elimination of transposable elements Botrytis cinerea
physiological function the organism contains 12 cutinases. High number of cutinases likely reflects its needs during post-invasion necrotrophic growth and overwintering as saprotrophic mycelia, and its ability to infect many different monocotyledonous genera asymptomatically Fusarium graminearum
physiological function the organism contains 17 cutinases. Preservation of a large number of diverse cutinases within the genome may provide the fungus with a great selective advantage to breach multiple, diverse grass cuticles, or may reflect its requirements to degrade different plant debris while overwintering as a soil saprotroph Pyricularia grisea