Any feedback?
Literature summary extracted from
- Diverse and common features of trehalases and their contributions to microbial trehalose metabolism (2020), Appl. Microbiol. Biotechnol., 104, 1837-1847.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.28 | additional information | enzyme Ntc1 activation by cAMP-dependent phosphorylation | Candida albicans |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.2.1.28 | gene ATH1, sequence comparisons | Saccharomyces cerevisiae |
| 3.2.1.28 | sequence comparisons | Aspergillus nidulans |
| 3.2.1.28 | sequence comparisons | Candida albicans |
| 3.2.1.28 | sequence comparisons | Escherichia coli |
| 3.2.1.28 | sequence comparisons | Mycolicibacterium smegmatis |
| 3.2.1.28 | sequence comparisons | Nakaseomyces glabratus |
| 3.2.1.28 | sequence comparisons | Neurospora crassa |
| 3.2.1.28 | sequence comparisons | Nostoc sp. |
| 3.2.1.28 | sequence comparisons | Rhodothermus sp. |
| 3.2.1.28 | sequence comparisons | Sulfolobus acidocaldarius |
| 3.2.1.28 | sequence comparisons | Thermoplasma acidophilum |
| 3.2.1.28 | sequence comparisons | Thermoplasma volcanium |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.28 | validamycin A | - |
Escherichia coli |  |
| 3.2.1.28 | validoxylamine | enzyme Tre37A binding structure analysis. In the structure with the inhibitor, the active site is completely covered by a loop that corresponds to the lid loop of Nth1 and contains Glu and Tyr residues (EY residues) | Escherichia coli | |
| 3.2.1.28 | validoxylamine | - |
Rhodothermus sp. | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.2.1.28 | cell wall | - |
Candida albicans | 5618 | - |
| 3.2.1.28 | cytoplasm | - |
Escherichia coli | 5737 | - |
| 3.2.1.28 | cytosol | - |
Saccharomyces cerevisiae | 5829 | - |
| 3.2.1.28 | extracellular | the enzyme is secreted | Nakaseomyces glabratus | - |
- |
| 3.2.1.28 | additional information | Escherichia coli can grow on trehalose as their sole source of carbon at either high or low osmolarities. Trehalose is transferred into the periplasm through the transmembrane protein LamB, which alternatively helps in transferring trehalose from the periplasm to outside the cells under high osmolarity | Escherichia coli | - |
- |
| 3.2.1.28 | periplasm | - |
Escherichia coli | - |
- |
| 3.2.1.28 | periplasm | - |
Rhodothermus sp. | - |
- |
| 3.2.1.28 | periplasm | - |
Saccharomyces cerevisiae | - |
- |
| 3.2.1.28 | vacuole | Ath1 is suggested to be located in vacuoles or at the surface of the cell | Saccharomyces cerevisiae | 5773 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.28 | Ca2+ | required for activity | Aspergillus nidulans | |
| 3.2.1.28 | Ca2+ | required for activity | Neurospora crassa | |
| 3.2.1.28 | Ca2+ | required for activity, Ca2+ binding within EF-hand-like motifs | Saccharomyces cerevisiae | |
| 3.2.1.28 | Ca2+ | required for activity | Saccharomyces cerevisiae | |
| 3.2.1.28 | Mg2+ | required | Mycolicibacterium smegmatis | |
| 3.2.1.28 | phosphate | required | Mycolicibacterium smegmatis | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Aspergillus nidulans | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Neurospora crassa | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Candida albicans | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Escherichia coli | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Nostoc sp. | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Rhodothermus sp. | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Saccharomyces cerevisiae | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Thermoplasma volcanium | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Nakaseomyces glabratus | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Mycobacterium tuberculosis | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Mycolicibacterium smegmatis | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Thermoplasma acidophilum | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Sulfolobus acidocaldarius | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Mycobacterium tuberculosis H37Rv | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Nakaseomyces glabratus CBS 138 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Aspergillus nidulans FGSC A4 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Mycolicibacterium smegmatis mc(2)155 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Neurospora crassa 74-OR23-1A | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Thermoplasma volcanium GSS1 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Sulfolobus acidocaldarius DSM 639 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Saccharomyces cerevisiae ATCC 204508 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Mycolicibacterium smegmatis ATCC 700084 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Thermoplasma acidophilum JCM 9062 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Candida albicans ATCC MYA-2876 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Nakaseomyces glabratus ATCC 2001 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Aspergillus nidulans ATCC 38163 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Mycobacterium tuberculosis ATCC 25618 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Neurospora crassa DSM 1257 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Neurospora crassa ATCC 24698 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Thermoplasma acidophilum ATCC 25905 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Sulfolobus acidocaldarius ATCC 33909 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Thermoplasma volcanium DSM 4299 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Neurospora crassa FGSC 987 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Aspergillus nidulans CBS 112.46 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Aspergillus nidulans NRRL 194 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Aspergillus nidulans M139 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Thermoplasma acidophilum NBRC 15155 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Thermoplasma acidophilum AMRC-C165 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Sulfolobus acidocaldarius JCM 8929 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Sulfolobus acidocaldarius NBRC 15157 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Sulfolobus acidocaldarius NCIMB 11770 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Neurospora crassa CBS 708.71 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Thermoplasma volcanium ATCC 51530 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Nakaseomyces glabratus BCRC 20586 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Nakaseomyces glabratus JCM 3761 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Nakaseomyces glabratus NBRC 0622 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Nakaseomyces glabratus NRRL Y-65 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Thermoplasma volcanium JCM 9571 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | Thermoplasma volcanium NBRC 15438 | - |
beta-D-glucose + alpha-D-glucose | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.28 | Aspergillus nidulans | O42777 | Aspergillus nidulans | - |
| 3.2.1.28 | Aspergillus nidulans ATCC 38163 | O42777 | Aspergillus nidulans | - |
| 3.2.1.28 | Aspergillus nidulans CBS 112.46 | O42777 | Aspergillus nidulans | - |
| 3.2.1.28 | Aspergillus nidulans FGSC A4 | O42777 | Aspergillus nidulans | - |
| 3.2.1.28 | Aspergillus nidulans M139 | O42777 | Aspergillus nidulans | - |
| 3.2.1.28 | Aspergillus nidulans NRRL 194 | O42777 | Aspergillus nidulans | - |
| 3.2.1.28 | Candida albicans | P52494 | - |
- |
| 3.2.1.28 | Candida albicans | Q5AAU5 | - |
- |
| 3.2.1.28 | Candida albicans ATCC MYA-2876 | Q5AAU5 | - |
- |
| 3.2.1.28 | Escherichia coli | P13482 | - |
- |
| 3.2.1.28 | Escherichia coli | P62601 | - |
- |
| 3.2.1.28 | Mycobacterium tuberculosis | P71741 | - |
- |
| 3.2.1.28 | Mycobacterium tuberculosis ATCC 25618 | P71741 | - |
- |
| 3.2.1.28 | Mycobacterium tuberculosis H37Rv | P71741 | - |
- |
| 3.2.1.28 | Mycolicibacterium smegmatis | A0R0W9 | - |
- |
| 3.2.1.28 | Mycolicibacterium smegmatis ATCC 700084 | A0R0W9 | - |
- |
| 3.2.1.28 | Mycolicibacterium smegmatis mc(2)155 | A0R0W9 | - |
- |
| 3.2.1.28 | Nakaseomyces glabratus | Q6FU75 | - |
- |
| 3.2.1.28 | Nakaseomyces glabratus ATCC 2001 | Q6FU75 | - |
- |
| 3.2.1.28 | Nakaseomyces glabratus BCRC 20586 | Q6FU75 | - |
- |
| 3.2.1.28 | Nakaseomyces glabratus CBS 138 | Q6FU75 | - |
- |
| 3.2.1.28 | Nakaseomyces glabratus JCM 3761 | Q6FU75 | - |
- |
| 3.2.1.28 | Nakaseomyces glabratus NBRC 0622 | Q6FU75 | - |
- |
| 3.2.1.28 | Nakaseomyces glabratus NRRL Y-65 | Q6FU75 | - |
- |
| 3.2.1.28 | Neurospora crassa | O42783 | - |
- |
| 3.2.1.28 | Neurospora crassa 74-OR23-1A | O42783 | - |
- |
| 3.2.1.28 | Neurospora crassa ATCC 24698 | O42783 | - |
- |
| 3.2.1.28 | Neurospora crassa CBS 708.71 | O42783 | - |
- |
| 3.2.1.28 | Neurospora crassa DSM 1257 | O42783 | - |
- |
| 3.2.1.28 | Neurospora crassa FGSC 987 | O42783 | - |
- |
| 3.2.1.28 | Nostoc sp. | - |
- |
- |
| 3.2.1.28 | Rhodothermus sp. | - |
- |
- |
| 3.2.1.28 | Saccharomyces cerevisiae | P48016 | - |
- |
| 3.2.1.28 | Saccharomyces cerevisiae | P32356 | - |
- |
| 3.2.1.28 | Saccharomyces cerevisiae | P35172 | - |
- |
| 3.2.1.28 | Saccharomyces cerevisiae ATCC 204508 | P32356 | - |
- |
| 3.2.1.28 | Saccharomyces cerevisiae ATCC 204508 | P48016 | - |
- |
| 3.2.1.28 | Saccharomyces cerevisiae ATCC 204508 | P35172 | - |
- |
| 3.2.1.28 | Sulfolobus acidocaldarius | Q4J7W0 | - |
- |
| 3.2.1.28 | Sulfolobus acidocaldarius | Q4J9D4 | - |
- |
| 3.2.1.28 | Sulfolobus acidocaldarius ATCC 33909 | Q4J7W0 | - |
- |
| 3.2.1.28 | Sulfolobus acidocaldarius ATCC 33909 | Q4J9D4 | - |
- |
| 3.2.1.28 | Sulfolobus acidocaldarius DSM 639 | Q4J7W0 | - |
- |
| 3.2.1.28 | Sulfolobus acidocaldarius DSM 639 | Q4J9D4 | - |
- |
| 3.2.1.28 | Sulfolobus acidocaldarius JCM 8929 | Q4J7W0 | - |
- |
| 3.2.1.28 | Sulfolobus acidocaldarius JCM 8929 | Q4J9D4 | - |
- |
| 3.2.1.28 | Sulfolobus acidocaldarius NBRC 15157 | Q4J7W0 | - |
- |
| 3.2.1.28 | Sulfolobus acidocaldarius NBRC 15157 | Q4J9D4 | - |
- |
| 3.2.1.28 | Sulfolobus acidocaldarius NCIMB 11770 | Q4J7W0 | - |
- |
| 3.2.1.28 | Sulfolobus acidocaldarius NCIMB 11770 | Q4J9D4 | - |
- |
| 3.2.1.28 | Thermoplasma acidophilum | Q9HLE2 | - |
- |
| 3.2.1.28 | Thermoplasma acidophilum AMRC-C165 | Q9HLE2 | - |
- |
| 3.2.1.28 | Thermoplasma acidophilum ATCC 25905 | Q9HLE2 | - |
- |
| 3.2.1.28 | Thermoplasma acidophilum JCM 9062 | Q9HLE2 | - |
- |
| 3.2.1.28 | Thermoplasma acidophilum NBRC 15155 | Q9HLE2 | - |
- |
| 3.2.1.28 | Thermoplasma volcanium | A0A0G4DBK0 | - |
- |
| 3.2.1.28 | Thermoplasma volcanium | Q978S7 | - |
- |
| 3.2.1.28 | Thermoplasma volcanium ATCC 51530 | Q978S7 | - |
- |
| 3.2.1.28 | Thermoplasma volcanium DSM 4299 | Q978S7 | - |
- |
| 3.2.1.28 | Thermoplasma volcanium GSS1 | A0A0G4DBK0 | - |
- |
| 3.2.1.28 | Thermoplasma volcanium GSS1 | Q978S7 | - |
- |
| 3.2.1.28 | Thermoplasma volcanium JCM 9571 | Q978S7 | - |
- |
| 3.2.1.28 | Thermoplasma volcanium NBRC 15438 | Q978S7 | - |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.2.1.28 | phosphoprotein | cAMP-dependent phosphorylation activation | Aspergillus nidulans |
| 3.2.1.28 | phosphoprotein | cAMP-dependent phosphorylation activation | Neurospora crassa |
| 3.2.1.28 | phosphoprotein | Ntc1 is activated through cAMP-dependent phosphorylation | Candida albicans |
| 3.2.1.28 | phosphoprotein | Nth1 activity is regulated through cAMP-dependent phosphorylation within 14-3-3 binding motifs, followed by 14-3-3 dimeric protein binding and Ca2+ binding within EF-hand-like motifs. Phosphorylated Nth1 (pNth1) exhibits its activity at neutral pH | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Aspergillus nidulans | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Neurospora crassa | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Candida albicans | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Escherichia coli | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Nostoc sp. | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Rhodothermus sp. | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Saccharomyces cerevisiae | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Thermoplasma volcanium | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Nakaseomyces glabratus | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Mycobacterium tuberculosis | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Mycolicibacterium smegmatis | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Thermoplasma acidophilum | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Sulfolobus acidocaldarius | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Mycobacterium tuberculosis H37Rv | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Nakaseomyces glabratus CBS 138 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Aspergillus nidulans FGSC A4 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Mycolicibacterium smegmatis mc(2)155 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Neurospora crassa 74-OR23-1A | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Thermoplasma volcanium GSS1 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Sulfolobus acidocaldarius DSM 639 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Saccharomyces cerevisiae ATCC 204508 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Mycolicibacterium smegmatis ATCC 700084 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Thermoplasma acidophilum JCM 9062 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Candida albicans ATCC MYA-2876 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Nakaseomyces glabratus ATCC 2001 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Aspergillus nidulans ATCC 38163 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Mycobacterium tuberculosis ATCC 25618 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Neurospora crassa DSM 1257 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Neurospora crassa ATCC 24698 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Thermoplasma acidophilum ATCC 25905 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Sulfolobus acidocaldarius ATCC 33909 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Thermoplasma volcanium DSM 4299 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Neurospora crassa FGSC 987 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Aspergillus nidulans CBS 112.46 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Aspergillus nidulans NRRL 194 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Aspergillus nidulans M139 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Thermoplasma acidophilum NBRC 15155 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Thermoplasma acidophilum AMRC-C165 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Sulfolobus acidocaldarius JCM 8929 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Sulfolobus acidocaldarius NBRC 15157 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Sulfolobus acidocaldarius NCIMB 11770 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Neurospora crassa CBS 708.71 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Thermoplasma volcanium ATCC 51530 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Nakaseomyces glabratus BCRC 20586 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Nakaseomyces glabratus JCM 3761 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Nakaseomyces glabratus NBRC 0622 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Nakaseomyces glabratus NRRL Y-65 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Thermoplasma volcanium JCM 9571 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Thermoplasma volcanium NBRC 15438 | beta-D-glucose + alpha-D-glucose | - |
? | |
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Escherichia coli | beta D-glucose + alpha-D-glucose | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.2.1.28 | monomer | Tre37A has an additional C-terminal region. The enzyme consists of an (alpha/alpha)6-barrel in which Asp312 and Glu496 play the roles of a catalytic acid and base, respectively, during the hydrolytic reaction | Escherichia coli |
| 3.2.1.28 | monomer | TreF has an extended region at its N-terminus | Escherichia coli |
| 3.2.1.28 | additional information | Nth1 possesses three parts: an N-terminal extension, a Ca2+-binding domain (CaBD), and a conserved C-terminal domain (CD). The N-terminal extension contains two parts, each of which possess a phosphorylation site (Ser60 or Ser83), function as 14-3-3 protein binding motifs, and are essential for Nth1 activation. The CaBD forms an EF-hand-like motif that is involved in Ca2+-dependent Nth1 activation, which is much weaker than 14-3-3 protein-dependent activation. The CD adopts an (alpha/alpha)6-barrel structure with two subdomains (I and II), and its active site is located in a deep pocket formed by loops. The catalytic residues, Asp478 and Glu674, are surrounded by the trehalase signature motifs 1 and 2, the former of which is part of subdomain I. Additionally, the long loop region that covers the active site as a lid, i.e. the lid loop, is between the EFhand-like motif of the CaBD and the CD and is thus involved in activity, with Glu and Tyr residues playing central roles in this function | Saccharomyces cerevisiae |
| 3.2.1.28 | additional information | the enzyme protein may consist of an N-terminal domain and a C-terminal domain (CD), that the N-terminal domain is a beta-sandwich structure and that the CD seems to adopt an (alpha/alpha)6-barreled structure based on a crystal structure of a bacterial GA | Mycolicibacterium smegmatis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.2.1.28 | ATC1 | - |
Candida albicans |
| 3.2.1.28 | ATC1 | - |
Nakaseomyces glabratus |
| 3.2.1.28 | Ath1 | - |
Saccharomyces cerevisiae |
| 3.2.1.28 | CaAtc1 | - |
Candida albicans |
| 3.2.1.28 | Cell wall acid trehalase | - |
Candida albicans |
| 3.2.1.28 | cell-linked acid trehalase | - |
Candida albicans |
| 3.2.1.28 | CgATH1 | - |
Nakaseomyces glabratus |
| 3.2.1.28 | cytosolic neutral trehalase | - |
Aspergillus nidulans |
| 3.2.1.28 | cytosolic neutral trehalase | - |
Neurospora crassa |
| 3.2.1.28 | cytosolic neutral trehalase | - |
Candida albicans |
| 3.2.1.28 | cytosolic neutral trehalase | - |
Saccharomyces cerevisiae |
| 3.2.1.28 | G15 trehalase | - |
Thermoplasma acidophilum |
| 3.2.1.28 | G15 trehalase | - |
Sulfolobus acidocaldarius |
| 3.2.1.28 | GH15 trehalase | - |
Mycobacterium tuberculosis |
| 3.2.1.28 | GH15 trehalase | - |
Mycolicibacterium smegmatis |
| 3.2.1.28 | GH15 trehalase | - |
Thermoplasma volcanium |
| 3.2.1.28 | GH37 trehalase | - |
Nostoc sp. |
| 3.2.1.28 | GH65 trehalase | - |
Candida albicans |
| 3.2.1.28 | MSMEG_4535 | - |
Mycolicibacterium smegmatis |
| 3.2.1.28 | neutral trehalase | - |
Aspergillus nidulans |
| 3.2.1.28 | neutral trehalase | - |
Neurospora crassa |
| 3.2.1.28 | NTC1 | - |
Candida albicans |
| 3.2.1.28 | NTH1 | - |
Saccharomyces cerevisiae |
| 3.2.1.28 | NTH2 | - |
Saccharomyces cerevisiae |
| 3.2.1.28 | periplasmic acid trehalase | - |
Saccharomyces cerevisiae |
| 3.2.1.28 | Rv2402 | - |
Mycobacterium tuberculosis |
| 3.2.1.28 | Ta0286 | - |
Thermoplasma acidophilum |
| 3.2.1.28 | Tre37A | - |
Escherichia coli |
| 3.2.1.28 | TreA | - |
Escherichia coli |
| 3.2.1.28 | treB | - |
Aspergillus nidulans |
| 3.2.1.28 | treB | - |
Neurospora crassa |
| 3.2.1.28 | TreF | - |
Escherichia coli |
| 3.2.1.28 | Treh | - |
Nostoc sp. |
| 3.2.1.28 | Treh | - |
Rhodothermus sp. |
| 3.2.1.28 | Treh | - |
Mycolicibacterium smegmatis |
| 3.2.1.28 | Treh1 | - |
Sulfolobus acidocaldarius |
| 3.2.1.28 | Treh2 | - |
Sulfolobus acidocaldarius |
| 3.2.1.28 | trehalase | - |
Aspergillus nidulans |
| 3.2.1.28 | trehalase | - |
Neurospora crassa |
| 3.2.1.28 | trehalase | - |
Candida albicans |
| 3.2.1.28 | trehalase | - |
Escherichia coli |
| 3.2.1.28 | trehalase | - |
Nostoc sp. |
| 3.2.1.28 | trehalase | - |
Rhodothermus sp. |
| 3.2.1.28 | trehalase | - |
Saccharomyces cerevisiae |
| 3.2.1.28 | trehalase | - |
Thermoplasma volcanium |
| 3.2.1.28 | trehalase | - |
Nakaseomyces glabratus |
| 3.2.1.28 | trehalase | - |
Mycobacterium tuberculosis |
| 3.2.1.28 | trehalase | - |
Mycolicibacterium smegmatis |
| 3.2.1.28 | trehalase | - |
Thermoplasma acidophilum |
| 3.2.1.28 | trehalase | - |
Sulfolobus acidocaldarius |
| 3.2.1.28 | trehalase 1 | - |
Sulfolobus acidocaldarius |
| 3.2.1.28 | trehalase 2 | - |
Sulfolobus acidocaldarius |
| 3.2.1.28 | trehalose-glucohydrolase | - |
Aspergillus nidulans |
| 3.2.1.28 | trehalose-glucohydrolase | - |
Neurospora crassa |
| 3.2.1.28 | trehalose-glucohydrolase | - |
Candida albicans |
| 3.2.1.28 | trehalose-glucohydrolase | - |
Escherichia coli |
| 3.2.1.28 | trehalose-glucohydrolase | - |
Nostoc sp. |
| 3.2.1.28 | trehalose-glucohydrolase | - |
Rhodothermus sp. |
| 3.2.1.28 | trehalose-glucohydrolase | - |
Saccharomyces cerevisiae |
| 3.2.1.28 | trehalose-glucohydrolase | - |
Thermoplasma volcanium |
| 3.2.1.28 | trehalose-glucohydrolase | - |
Nakaseomyces glabratus |
| 3.2.1.28 | trehalose-glucohydrolase | - |
Mycobacterium tuberculosis |
| 3.2.1.28 | trehalose-glucohydrolase | - |
Mycolicibacterium smegmatis |
| 3.2.1.28 | trehalose-glucohydrolase | - |
Thermoplasma acidophilum |
| 3.2.1.28 | trehalose-glucohydrolase | - |
Sulfolobus acidocaldarius |
| 3.2.1.28 | TreHperi | - |
Rhodothermus sp. |
| 3.2.1.28 | TVG1381191 | - |
Thermoplasma volcanium |
| 3.2.1.28 | Tvn1315 | - |
Thermoplasma volcanium |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.28 | 5.5 | 6 | - |
Escherichia coli |
| 3.2.1.28 | 7 | - |
- |
Saccharomyces cerevisiae |
| 3.2.1.28 | 7 | - |
about, neutral pH optimum | Saccharomyces cerevisiae |
Expression
| EC Number | Organism | Comment | Expression |
|---|---|---|---|
| 3.2.1.28 | Escherichia coli | enhanced production of trehalose in Escherichia coli by homologous expression of otsBA in the presence of the trehalase inhibitor, validamycin A, at high osmolarity | up |
| 3.2.1.28 | Escherichia coli | enhanced trehalose production improves growth of Escherichia coli under osmotic stress | up |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.2.1.28 | evolution | in trehalose metabolism, direct trehalose-hydrolyzing enzymes are known as trehalases, which are reported for bacteria, archaea, and eukaryotes, and are classified into glycoside hydrolase 37 (GH37), GH65, and GH15 families according to the Carbohydrate-Active enZyme (CAZy) database. The catalytic domains (CDs) of these enzymes commonly share (alpha/alpha)6-barrel structures and have two amino acid residues, Asp and/or Glu, that function as catalytic residues in an inverting mechanism. Emericella nidulans trehalase belongs to the G37 family (clan GH-G). Glu and Tyr residues (EY residues) are conserved in all GH37 trehalases except for Nostoc TreH (SF) and Rhodothermus TreH (RY). Neutral trehalases from Aspergillus nidulans and Neurospora crassa adopt similar features, such as cAMP-dependent phosphorylation activation and Ca2+ requirement for activity | Aspergillus nidulans |
| 3.2.1.28 | evolution | in trehalose metabolism, direct trehalose-hydrolyzing enzymes are known as trehalases, which are reported for bacteria, archaea, and eukaryotes, and are classified into glycoside hydrolase 37 (GH37), GH65, and GH15 families according to the Carbohydrate-Active enZyme (CAZy) database. The catalytic domains (CDs) of these enzymes commonly share (alpha/alpha)6-barrel structures and have two amino acid residues, Asp and/or Glu, that function as catalytic residues in an inverting mechanism. Neurospora crassa trehalase belongs to the G37 family (clan GH-G). Glu and Tyr residues (EY residues) are conserved in all GH37 trehalases except for Nostoc TreH (SF) and Rhodothermus TreH (RY). Neutral trehalases from Aspergillus nidulans and Neurospora crassa adopt similar features, such as cAMP-dependent phosphorylation activation and Ca2+ requirement for activity | Neurospora crassa |
| 3.2.1.28 | evolution | in trehalose metabolism, direct trehalose-hydrolyzing enzymes are known as trehalases, which are reported for bacteria, archaea, and eukaryotes, and are classified into glycoside hydrolase 37 (GH37), GH65, and GH15 families according to the Carbohydrate-Active enZyme (CAZy) database. The catalytic domains (CDs) of these enzymes commonly share (alpha/alpha)6-barrel structures and have two amino acid residues, Asp and/or Glu, that function as catalytic residues in an inverting mechanism. Candida albicans trehalase belongs to the G37 family (clan GH-G). Glu and Tyr residues (EY residues) are conserved in all GH37 trehalases except for Nostoc TreH (SF) and Rhodothermus TreH (RY) | Candida albicans |
| 3.2.1.28 | evolution | in trehalose metabolism, direct trehalose-hydrolyzing enzymes are known as trehalases, which are reported for bacteria, archaea, and eukaryotes, and are classified into glycoside hydrolase 37 (GH37), GH65, and GH15 families according to the Carbohydrate-Active enZyme (CAZy) database. The catalytic domains (CDs) of these enzymes commonly share (alpha/alpha)6-barrel structures and have two amino acid residues, Asp and/or Glu, that function as catalytic residues in an inverting mechanism. Escherichia coli trehalase belongs to the G37 family (clan GH-G). Glu and Tyr residues (EY residues) are conserved in all GH37 trehalases except for Nostoc TreH (SF) and Rhodothermus TreH (RY) | Escherichia coli |
| 3.2.1.28 | evolution | in trehalose metabolism, direct trehalose-hydrolyzing enzymes are known as trehalases, which are reported for bacteria, archaea, and eukaryotes, and are classified into glycoside hydrolase 37 (GH37), GH65, and GH15 families according to the Carbohydrate-Active enZyme (CAZy) database. The catalytic domains (CDs) of these enzymes commonly share (alpha/alpha)6-barrel structures and have two amino acid residues, Asp and/or Glu, that function as catalytic residues in an inverting mechanism. Nostoc trehalase belongs to the G37 family (clan GH-G). Glu and Tyr residues (EY residues) are conserved in all GH37 trehalases except for Nostoc TreH (SF) and Rhodothermus TreH (RY). The enzyme from Nostoc belongs to the GH37 family of glycoside hydrolases | Nostoc sp. |
| 3.2.1.28 | evolution | in trehalose metabolism, direct trehalose-hydrolyzing enzymes are known as trehalases, which are reported for bacteria, archaea, and eukaryotes, and are classified into glycoside hydrolase 37 (GH37), GH65, and GH15 families according to the Carbohydrate-Active enZyme (CAZy) database. The catalytic domains (CDs) of these enzymes commonly share (alpha/alpha)6-barrel structures and have two amino acid residues, Asp and/or Glu, that function as catalytic residues in an inverting mechanism. Rhodothermus trehalase belongs to the G37 family (clan GH-G). Glu and Tyr residues (EY residues) are conserved in all GH37 trehalases except for Nostoc TreH (SF) and Rhodothermus TreH (RY) | Rhodothermus sp. |
| 3.2.1.28 | evolution | in trehalose metabolism, direct trehalose-hydrolyzing enzymes are known as trehalases, which are reported for bacteria, archaea, and eukaryotes, and are classified into glycoside hydrolase 37 (GH37), GH65, and GH15 families according to the Carbohydrate-Active enZyme (CAZy) database. The catalytic domains (CDs) of these enzymes commonly share (alpha/alpha)6-barrel structures and have two amino acid residues, Asp and/or Glu, that function as catalytic residues in an inverting mechanism. Rhodothermus trehalase belongs to the G37 family (clan GH-G). Glu and Tyr residues (EY residues) are conserved in all GH37 trehalases except for Nostoc TreH (SF) and Rhodothermus TreH (RY). Saccharomyces cerevisiae enzyme Ath1 belongs to the glycoside hydrolase family 37, GH37 | Saccharomyces cerevisiae |
| 3.2.1.28 | evolution | in trehalose metabolism, direct trehalose-hydrolyzing enzymes are known as trehalases, which are reported for bacteria, archaea, and eukaryotes, and are classified into glycoside hydrolase 37 (GH37), GH65, and GH15 families according to the Carbohydrate-Active enZyme (CAZy) database. The catalytic domains (CDs) of these enzymes commonly share (alpha/alpha)6-barrel structures and have two amino acid residues, Asp and/or Glu, that function as catalytic residues in an inverting mechanism. Rhodothermus trehalase belongs to the G37 family (clan GH-G). Glu and Tyr residues (EY residues) are conserved in all GH37 trehalases except for Nostoc TreH (SF) and Rhodothermus TreH (RY) | Thermoplasma volcanium |
| 3.2.1.28 | evolution | in trehalose metabolism, direct trehalose-hydrolyzing enzymes are known as trehalases, which are reported for bacteria, archaea, and eukaryotes, and are classified into glycoside hydrolase 37 (GH37), GH65, and GH15 families according to the carbohydrate-active enZyme (CAZy) database. The catalytic domains (CDs) of these enzymes commonly share (alpha/alpha)6-barrel structures and have two amino acid residues, Asp and/or Glu, that function as catalytic residues in an inverting mechanism. Saccharomyces cerevisiae trehalases belong to the G37 family (clan GH-G). Glu and Tyr residues (EY residues) are conserved in all GH37 trehalases except for Nostoc TreH (SF) and Rhodothermus TreH (RY) | Saccharomyces cerevisiae |
| 3.2.1.28 | evolution | in trehalose metabolism, direct trehalose-hydrolyzing enzymes are known as trehalases, which are reported for bacteria, archaea, and eukaryotes, and are classified into glycoside hydrolase 37 (GH37), GH65, and GH15 families according to the Carbohydrate-Active enZyme (CAZy) database. The catalytic domains (CDs) of these enzymes commonly share (alpha/alpha)6-barrel structures and have two amino acid residues, Asp and/or Glu, that function as catalytic residues in an inverting mechanism. Rhodothermus trehalase belongs to the G37 family (clan GH-G). Glu and Tyr residues (EY residues) are conserved in all GH37 trehalases except for Nostoc TreH (SF) and Rhodothermus TreH (RY). Enzyme Atc1 belongs to the glycoside hydrolase family 65, GH 65 | Candida albicans |
| 3.2.1.28 | evolution | in trehalose metabolism, direct trehalose-hydrolyzing enzymes are known as trehalases, which are reported for bacteria, archaea, and eukaryotes, and are classified into glycoside hydrolase 37 (GH37), GH65, and GH15 families according to the Carbohydrate-Active enZyme (CAZy) database. The catalytic domains (CDs) of these enzymes commonly share (alpha/alpha)6-barrel structures and have two amino acid residues, Asp and/or Glu, that function as catalytic residues in an inverting mechanism. Rhodothermus trehalase belongs to the G37 family (clan GH-G). Glu and Tyr residues (EY residues) are conserved in all GH37 trehalases except for Nostoc TreH (SF) and Rhodothermus TreH (RY). Enzyme Atc1 from Candida glabrata belongs to the glycoside hydrolase family 65, GH65 | Nakaseomyces glabratus |
| 3.2.1.28 | evolution | in trehalose metabolism, direct trehalose-hydrolyzing enzymes are known as trehalases, which are reported for bacteria, archaea, and eukaryotes, and are classified into glycoside hydrolase 37 (GH37), GH65, and GH15 families according to the Carbohydrate-Active enZyme (CAZy) database. The catalytic domains (CDs) of these enzymes commonly share (alpha/alpha)6-barrel structures and have two amino acid residues, Asp and/or Glu, that function as catalytic residues in an inverting mechanism. Mycobacterium tuberculosis trehalase belongs to the G15 family (clan GH-L) | Mycobacterium tuberculosis |
| 3.2.1.28 | evolution | in trehalose metabolism, direct trehalose-hydrolyzing enzymes are known as trehalases, which are reported for bacteria, archaea, and eukaryotes, and are classified into glycoside hydrolase 37 (GH37), GH65, and GH15 families according to the Carbohydrate-Active enZyme (CAZy) database. The catalytic domains (CDs) of these enzymes commonly share (alpha/alpha)6-barrel structures and have two amino acid residues, Asp and/or Glu, that function as catalytic residues in an inverting mechanism. Mycobacterium smegmatis trehalase belongs to the G15 family (clan GH-L) | Mycolicibacterium smegmatis |
| 3.2.1.28 | evolution | in trehalose metabolism, direct trehalose-hydrolyzing enzymes are known as trehalases, which are reported for bacteria, archaea, and eukaryotes, and are classified into glycoside hydrolase 37 (GH37), GH65, and GH15 families according to the Carbohydrate-Active enZyme (CAZy) database. The catalytic domains (CDs) of these enzymes commonly share (alpha/alpha)6-barrel structures and have two amino acid residues, Asp and/or Glu, that function as catalytic residues in an inverting mechanism. The trehalase from thermoacidophilic euryarchaeon Thermoplasma volcanium belongs to the G15 family (clan GH-L) | Thermoplasma volcanium |
| 3.2.1.28 | evolution | in trehalose metabolism, direct trehalose-hydrolyzing enzymes are known as trehalases, which are reported for bacteria, archaea, and eukaryotes, and are classified into glycoside hydrolase 37 (GH37), GH65, and GH15 families according to the Carbohydrate-Active enZyme (CAZy) database. The catalytic domains (CDs) of these enzymes commonly share (alpha/alpha)6-barrel structures and have two amino acid residues, Asp and/or Glu, that function as catalytic residues in an inverting mechanism. Thermoacidophilic euryarchaeon Thermoplasma acidophilum trehalase belongs to the G15 family (clan GH-L) | Thermoplasma acidophilum |
| 3.2.1.28 | evolution | in trehalose metabolism, direct trehalose-hydrolyzing enzymes are known as trehalases, which are reported for bacteria, archaea, and eukaryotes, and are classified into glycoside hydrolase 37 (GH37), GH65, and GH15 families according to the Carbohydrate-Active enZyme (CAZy) database. The catalytic domains (CDs) of these enzymes commonly share (alpha/alpha)6-barrel structures and have two amino acid residues, Asp and/or Glu, that function as catalytic residues in an inverting mechanism. Thermoacidophilic euryarchaeon Thermoplasma acidophilum trehalase belongs to the G15 family (clan GH-L) | Sulfolobus acidocaldarius |
| 3.2.1.28 | evolution | in trehalose metabolism, direct trehalose-hydrolyzing enzymes are known as trehalases, which are reported for bacteria, archaea, and eukaryotes, and are classified into glycoside hydrolase 37 (GH37), GH65, and GH15 families according to the Carbohydrate-Active enZyme (CAZy) database. The catalytic domains (CDs) of these enzymes commonly share (alpha/alpha)6-barrel structures and have two amino acid residues, Asp and/or Glu, that function as catalytic residues in an inverting mechanism. Crenarchaeon Thermoplasma acidophilum trehalase belongs to the G15 family (clan GH-L) | Sulfolobus acidocaldarius |
| 3.2.1.28 | malfunction | enhanced trehalose production improves growth of Escherichia coli under osmotic stress | Escherichia coli |
| 3.2.1.28 | malfunction | deletion of TPS1 reveals Ath1pdependent trehalose mobilization. Deletion of the ATH1 gene in Saccharomyces cerevisiae prevents growth on trehalose. Ath1 gene-deleted yeast cells lack the ability to grow on trehalose as a carbon source. The Ath1 gene-defective strain also accumulates increased levels of cellular trehalose, leading to an increase in tolerance of adverse conditions such as dehydration, freezing, and toxic levels of ethanol. Disruption of the yeast ATH1 gene confers better survival after dehydration, freezing, and ethanol shock | Saccharomyces cerevisiae |
| 3.2.1.28 | malfunction | disruption of the Candida albicans ATC1 gene encoding the cell-linked acid trehalase decreases hypha formation and infectivity without affecting resistance to oxidative stress. In addition, atc1 null mutants display strongly reduced pathogenicity in a systemic murine model, suggesting that Atc1 plays some roles in dimorphism, infectivity, stress resistance, and virulence | Candida albicans |
| 3.2.1.28 | metabolism | in mycobacteria (and the related corynebacteria), trehalose has attracted particular attention because of its incorporation into cell wall mycolic acids, which are involved in pathogenesis and immune system evasion | Mycobacterium tuberculosis |
| 3.2.1.28 | metabolism | in mycobacteria (and the related corynebacteria), trehalose has attracted particular attention because of its incorporation into cell wall mycolic acids, which are involved in pathogenesis and immune system evasion | Mycolicibacterium smegmatis |
| 3.2.1.28 | additional information | Asp312 and Glu496 play the roles of a catalytic acid and base, respectively, during the hydrolytic reaction | Escherichia coli |
| 3.2.1.28 | physiological function | trehalase hydrolyzes trehalose to produce two glucose molecules | Aspergillus nidulans |
| 3.2.1.28 | physiological function | trehalase hydrolyzes trehalose to produce two glucose molecules | Neurospora crassa |
| 3.2.1.28 | physiological function | trehalase hydrolyzes trehalose to produce two glucose molecules. Trehalase, Ntc1 is not involved in Candida albicans pathogenicity but is required for the physiological mobilization of endogenous trehalose | Candida albicans |
| 3.2.1.28 | physiological function | trehalase hydrolyzes trehalose to produce two glucose molecules | Escherichia coli |
| 3.2.1.28 | physiological function | trehalase hydrolyzes trehalose to produce two glucose molecules | Nostoc sp. |
| 3.2.1.28 | physiological function | trehalase hydrolyzes trehalose to produce two glucose molecules | Rhodothermus sp. |
| 3.2.1.28 | physiological function | trehalase hydrolyzes trehalose to produce two glucose molecules. Protective role of trehalose during heat stress in Saccharomyces cerevisiae, trehalose protective mechanism. Ath1 may have a role in degrading external trehalose during stress recover; during stress, trehalose synthesized in cytosol is transported to the outside through Agt1 to protect the external face of lipid bilayer, when cells return to non-stress conditions, the trehalose is degraded by Ath1 | Saccharomyces cerevisiae |
| 3.2.1.28 | physiological function | trehalase hydrolyzes trehalose to produce two glucose molecules | Thermoplasma volcanium |
| 3.2.1.28 | physiological function | trehalase hydrolyzes trehalose to produce two glucose molecules. Enzyme Nth1 activity is regulated at posttranslational levels. Nth1 activity is regulated through cAMP-dependent phosphorylation within 14-3-3 binding motifs, followed by 14-3-3 dimeric protein binding and Ca2+ binding within EF-hand-like motifs. Thus, phosphorylated Nth1 (pNth1) exhibits its activity at neutral pH (pH optimum of 7.0) | Saccharomyces cerevisiae |
| 3.2.1.28 | physiological function | trehalase hydrolyzes trehalose to produce two glucose molecules | Saccharomyces cerevisiae |
| 3.2.1.28 | physiological function | the ATC1 gene encodes a cell wall-linked acid trehalase required for growth on trehalose in Candida albicans. Trehalase hydrolyzes trehalose to produce two glucose molecules. Atc1 is localized in the cell wall and is required to hydrolyze exogenous trehalose as a carbon source for growth | Candida albicans |
| 3.2.1.28 | physiological function | trehalase hydrolyzes trehalose to produce two glucose molecules. Secretion of the acid trehalase encoded by the CgATH1 gene allows trehalose fermentation by Candida glabrata | Nakaseomyces glabratus |
| 3.2.1.28 | physiological function | trehalase hydrolyzes trehalose to produce two glucose molecules | Mycobacterium tuberculosis |
| 3.2.1.28 | physiological function | trehalase hydrolyzes trehalose to produce two glucose molecules | Mycolicibacterium smegmatis |
| 3.2.1.28 | physiological function | trehalase hydrolyzes trehalose to produce two glucose molecules | Thermoplasma acidophilum |
| 3.2.1.28 | physiological function | trehalase hydrolyzes trehalose to produce two glucose molecules, trehalase catalyzes trehalose degradation in the thermoacidophilic Crenarchaeon. Two trehalose-hydrolyzing enzymes from Sulfolobus acidocaldarius exhibit distinct activities and affinities toward trehalose | Sulfolobus acidocaldarius |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
