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Literature summary for 3.1.1.74 extracted from
- Catalysis by Glomerella cingulata cutinase requires conformational cycling between the active and inactive states of its catalytic triad (2009), J. Mol. Biol., 385, 226-235.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli Origami B(DE3) | Fusarium solani |
| expressed in Escherichia coli strain Origami B(DE3) | Fusarium solani |
| expressed in Escherichia coli strain Origami B(DE3) | Colletotrichum gloeosporioides |
| mutant H204N overexpressed in Escherichia coli Origami B(DE3) | Colletotrichum gloeosporioides |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
- |
Fusarium solani |
- |
Colletotrichum gloeosporioides |
| in the absence and in the presence of the inhibitors diethyl p-nitrophenyl phosphate (belongs to space group P21) and 3-phenethylthio-1,1,1-trifluoropropan-2-one (belongs to space group P212121), to resolutions of 2.6 and 2.3 A, respectively. Apo-cutinase, 1.9 A resolution, belongs to space group P41212 with one subunit in the asymmetric unit with unit cell parameters a = 60, b = 60, c = 86 A, respectively. The catalytic triad (Ser136, Asp191, and His204) adopts an unusual configuration with the putative essential histidine His204 swung out of the active site into a position where it is unable to participate in catalysis, with the imidazole ring 11 A away from its expected position | Colletotrichum gloeosporioides |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| H204N | site-directed mutant, constructed, overexpressed, and purified | Colletotrichum gloeosporioides |
| H204N | is catalytically inactive. Is not covalently modified by a 4fold excess of diethyl p-nitrophenyl phosphate, in contrast to the wild-type | Colletotrichum gloeosporioides |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 3-phenethylthio-1,1,1-trifluoropropan-2-one | - |
Colletotrichum gloeosporioides |  |
| 3-phenethylthio-1,1,1-trifluoropropan-2-one | - |
Fusarium solani | |
| Diethyl p-nitrophenyl phosphate | E600 | Colletotrichum gloeosporioides | |
| Diethyl p-nitrophenyl phosphate | E600 | Fusarium solani | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Fusarium solani | - |
- |
| extracellular | - |
Colletotrichum gloeosporioides | - |
- |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 21010 | - |
after preincubation with 20 mM diethyl p-nitrophenyl phosphate, the peak at 21010 Da represents the nonmodified H204N mutant, mass spectrometry | Colletotrichum gloeosporioides |
| 21010 | - |
H204N site-directed mutant, mass spectrometry | Colletotrichum gloeosporioides |
| 21010 | - |
H204N mutant, mass spectrometry | Colletotrichum gloeosporioides |
| 21030 | - |
wild type, mass spectrometry | Colletotrichum gloeosporioides |
| 21030 | - |
wild-type, mass spectrometry | Colletotrichum gloeosporioides |
| 21170 | - |
after preincubation with 20 mM diethyl p-nitrophenyl phosphate, the peak at 21168 Da represents the covalently modified wild-type cutinase, mass spectrometry | Colletotrichum gloeosporioides |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Colletotrichum gloeosporioides | P11373 | - |
- |
| Fusarium solani | P00590 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Fusarium solani |
- |
Colletotrichum gloeosporioides |
| by ion-exchange chromatography | Colletotrichum gloeosporioides |
| by nickel-affinity chromatography | Fusarium solani |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | during its catalytic cycle, cutinase undergoes a significant conformational rearrangement converting the loop bearing the histidine from an inactive conformation, in which the histidine of the triad is solvent exposed, to an active conformation, in which the triad assumes a classic configuration. Major difference between the structures is in the position of the loop connecting beta5 and alpha5 (Gly196Phe205 in Glomerella cingulata cutinase and Gly180Leu189 in Fusarium solani cutinase). Consequence of the repositioning of the loop is that the active-site regions of the enzymes differ substantially in the location of the putative catalytic histidine (His188 of Fusarium solani cutinase and His204 of Glomerella cingulata cutinase) | Colletotrichum gloeosporioides | ? | - |
? | |
| additional information | major difference between the structures is in the position of the loop connecting beta5 and alpha5 (Gly196Phe205 in Glomerella cingulata cutinase and Gly180Leu189 in Fusarium solani cutinase). Consequence of the repositioning of the loop is that the active-site regions of the enzymes differ substantially in the location of the putative catalytic histidine (His188 of Fusarium solani cutinase and His204 of Glomerella cingulata cutinase) | Fusarium solani | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | - |
Fusarium solani |
| monomer | - |
Colletotrichum gloeosporioides |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| cutinase | - |
Fusarium solani |
| cutinase | - |
Colletotrichum gloeosporioides |
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Release 2023.1 (January 2023)
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