A8QPD8 · CUTI1_TRIHA

Function

function

Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:18987860).
May degrade cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:18987860).
May also degrade suberin, a specialized macromolecule found in the cell wall of various plant tissues (PubMed:18987860).

Catalytic activity

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.33 mMp-nitrophenyl acetate825
0.57 mMp-nitrophenyl butyrate825
0.82 mMp-nitrophenyl valerate825
0.085 mMp-nitrophenyl palmitate837

pH Dependence

Optimum pH is 7.5-8.

Features

Showing features for site, active site.

TypeIDPosition(s)Description
Site90Transition state stabilizer
Active site164Nucleophile
Site165Transition state stabilizer
Active site216
Active site229Proton donor/acceptor

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functioncutinase activity

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Cutinase cut1
  • EC number
  • Alternative names
    • Thcut1

Gene names

    • Name
      cut1

Organism names

  • Taxonomic identifier
  • Strain
    • ATCC 48131 / CBS 354.33 / CECT 2413 / VTT D-80150
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Hypocreaceae > Trichoderma

Accessions

  • Primary accession
    A8QPD8

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

TypeIDPosition(s)Description
Signal1-17
ChainPRO_500511751118-248Cutinase cut1
Disulfide bond79↔153
Disulfide bond212↔219

Post-translational modification

The 2 disulfide bonds play a critical role in holding the catalytic residues in juxta-position; reduction of the disulfide bridges results in the complete inactivation of the enzyme.

Keywords

Expression

Induction

Induced during growth on olive oil (PubMed:18987860).
Induced during growth on the lipidic carbon source 16-hydroxyhexadecanoic acid (synthetic cutin monomer) (PubMed:18987860).
Induced during growth on plant material (PubMed:18987860).
Induced during growth on pectin (PubMed:18987860).
Repressed during growth on glucose carbon source (PubMed:18987860).

Structure

Family & Domains

Sequence similarities

Belongs to the cutinase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    248
  • Mass (Da)
    26,007
  • Last updated
    2008-01-15 v1
  • Checksum
    3CDEF12D896F9DE6
MRSLSLFTALLAGQAFAYPKPVLQSSTRRDWPTINEFLTELAEIMPIGDTVSAACDLIGDAEDVAADLFDISNTENDACGDVTVLFARGTCDPGNVGVLVGPWFFNSLETALPNKKVGVKGVPYPASVQGFLSGSVQPGIDMANQIKSVISSCPNTKLVLGGYSQGSMVVHNAASNLDAATMAKVSAVVLFGDPYDGRPVANYDASKVLVVCHDGDNICQGGDFILLPHLTYAEDADTAAAFVKPLVS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
EF108302
EMBL· GenBank· DDBJ
ABN48556.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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