Enzymes
| UniProtKB help_outline | 1 proteins |
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- Name help_outline D-cellohexaose Identifier CHEBI:143194 Charge 0 Formula C36H62O31 InChIKeyhelp_outline OCIBBXPLUVYKCH-UOHXBEGVSA-N SMILEShelp_outline OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)[C@H](O[C@H]3[C@H](O)[C@@H](O)[C@H](O[C@H]4[C@H](O)[C@@H](O)[C@H](O[C@H]5[C@H](O)[C@@H](O)[C@H](O[C@H]6[C@H](O)[C@@H](O)C(O)O[C@@H]6CO)O[C@@H]5CO)O[C@@H]4CO)O[C@@H]3CO)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline O2 Identifier CHEBI:15379 (CAS: 7782-44-7) help_outline Charge 0 Formula O2 InChIKeyhelp_outline MYMOFIZGZYHOMD-UHFFFAOYSA-N SMILEShelp_outline O=O 2D coordinates Mol file for the small molecule Search links Involved in 2,851 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline D-cellohexaono-1,5-lactone Identifier CHEBI:143174 Charge 0 Formula C36H60O31 InChIKeyhelp_outline QYBQUOGVPYOWBW-WLFNWXPVSA-N SMILEShelp_outline [C@H]1([C@H](O[C@@H](O[C@@H]2[C@H](OC(=O)[C@@H]([C@H]2O)O)CO)[C@@H]([C@H]1O)O)CO)O[C@@H]3O[C@@H]([C@@H](O[C@@H]4O[C@@H]([C@@H](O[C@@H]5O[C@@H]([C@@H](O[C@@H]6O[C@@H]([C@@H](O)[C@@H]([C@H]6O)O)CO)[C@@H]([C@H]5O)O)CO)[C@@H]([C@H]4O)O)CO)[C@@H]([C@H]3O)O)CO 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O2 Identifier CHEBI:16240 (CAS: 7722-84-1) help_outline Charge 0 Formula H2O2 InChIKeyhelp_outline MHAJPDPJQMAIIY-UHFFFAOYSA-N SMILEShelp_outline [H]OO[H] 2D coordinates Mol file for the small molecule Search links Involved in 461 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:59668 | RHEA:59669 | RHEA:59670 | RHEA:59671 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Structural characterization of glucooligosaccharide oxidase from Acremonium strictum.
Lee M.H., Lai W.L., Lin S.F., Hsu C.S., Liaw S.H., Tsai Y.C.
Glucooligosaccharide oxidase from Acremonium strictum was screened for potential applications in oligosaccharide acid production and carbohydrate detection. This protein is a unique covalent flavoenzyme which catalyzes the oxidation of a variety of carbohydrates with high selectivity for cello- an ... >> More
Glucooligosaccharide oxidase from Acremonium strictum was screened for potential applications in oligosaccharide acid production and carbohydrate detection. This protein is a unique covalent flavoenzyme which catalyzes the oxidation of a variety of carbohydrates with high selectivity for cello- and maltooligosaccharides. Kinetic measurements suggested that this enzyme possesses an open carbohydrate-binding groove, which is mainly composed of two glucosyl-binding subsites. The encoding gene was subsequently cloned, and one intron was detected in the genomic DNA. Large amounts of active enzymes were expressed in Pichia pastoris, with a yield of 300 mg per liter medium. The protein was predicted to share structural homology with plant cytokinin dehydrogenase and related flavoproteins that share a conserved flavin adenine dinucleotide (FAD)-binding domain. The closest sequence matches are those of plant berberine bridge enzyme-like proteins, particularly the characteristic flavinylation site. Unexpectedly, mutation of the putative FAD-attaching residue, H70, to alanine, serine, cysteine, and tyrosine did not abolish the covalent FAD linkage and had little effect on the Km. Instead, the variants displayed kcat values that were 50-to 600-fold lower, indicating that H70 is crucial for efficient redox catalysis, perhaps through modulation of the oxidative power of the flavin. << Less
Appl. Environ. Microbiol. 71:8881-8887(2005) [PubMed] [EuropePMC]
This publication is cited by 17 other entries.