Enzymes
| UniProtKB help_outline | 2 proteins |
| Enzyme class help_outline |
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| GO Molecular Function help_outline |
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- Name help_outline α,α-trehalose Identifier CHEBI:16551 (Beilstein: 1292766; CAS: 99-20-7) help_outline Charge 0 Formula C12H22O11 InChIKeyhelp_outline HDTRYLNUVZCQOY-LIZSDCNHSA-N SMILEShelp_outline OC[C@H]1O[C@H](O[C@H]2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2O)[C@H](O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 14 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline phosphate Identifier CHEBI:43474 Charge -2 Formula HO4P InChIKeyhelp_outline NBIIXXVUZAFLBC-UHFFFAOYSA-L SMILEShelp_outline OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 992 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline β-D-glucose 1-phosphate Identifier CHEBI:57684 (Beilstein: 1688547) help_outline Charge -2 Formula C6H11O9P InChIKeyhelp_outline HXXFSFRBOHSIMQ-DVKNGEFBSA-L SMILEShelp_outline OC[C@H]1O[C@@H](OP([O-])([O-])=O)[C@H](O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 9 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline D-glucose Identifier CHEBI:4167 (Beilstein: 1281604; CAS: 2280-44-6) help_outline Charge 0 Formula C6H12O6 InChIKeyhelp_outline WQZGKKKJIJFFOK-GASJEMHNSA-N SMILEShelp_outline OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 161 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:23512 | RHEA:23513 | RHEA:23514 | RHEA:23515 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Characterization of trehalose phosphorylase from Bacillus stearothermophilus SK-1 and nucleotide sequence of the corresponding gene.
Inoue Y., Ishii K., Tomita T., Yatake T., Fukui F.
A bacterial trehalose phosphorylase (TPase; EC 2.4.1.64) was purified from the culture supernatant of Bacillus stearothermophilus SK-1 to apparent homogeneity, and some properties were investigated. Furthermore, a gene from SK-1 responsible for the TPase was cloned by Southern hybridization with a ... >> More
A bacterial trehalose phosphorylase (TPase; EC 2.4.1.64) was purified from the culture supernatant of Bacillus stearothermophilus SK-1 to apparent homogeneity, and some properties were investigated. Furthermore, a gene from SK-1 responsible for the TPase was cloned by Southern hybridization with a degenerate oligonucleotide probe synthesized on the basis of the N-terminal sequence of the purified enzyme. The Mr of the enzyme was estimated to be 150,000 by gel filtration and 83,000 by SDS-PAGE, so the enzyme is likely to be a homodimer. The enzyme had optimum activity at pH 7.0-8.0 or nearby and the optimum temperature was about 75 degrees C. The deduced amino acid sequence of the SK-1 TPase encodes a theoretical protein with a Mr of 87,950. Alignment of amino acid sequences with a maltose phosphorylase from Lactobacillus brevis the crystal structure and active site of which had been analyzed suggested that these two phosphorylases evolved from a common ancestor. The Escherichia coli cells harboring the plasmid containing the cloned TPase gene had about 100 times the activity of SK-1. << Less
Biosci. Biotechnol. Biochem. 66:1835-1843(2002) [PubMed] [EuropePMC]
Comments
Published in: "Purification and characterization of thermostable trehalose phosphorylase from Thermoanaerobium brockii." Chaen H., Nakada T., Nishimoto T., Kuroda N., Fukuda S., Sugimoto T., Kurimoto M., Tsujisaka Y. J. Appl. Glycosci. 46:399-405(1999)