Summary: Cholesterol oxidase, substrate-binding
This is the Wikipedia entry entitled "Cholesterol oxidase". More...
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Cholesterol oxidase Edit Wikipedia article
|PDB structures||RCSB PDB PDBe PDBsum|
|Gene Ontology||AmiGO / EGO|
|Cholesterol oxidase substrate-binding domain|
crystal structure of cholesterol oxidase from b.sterolicum
- cholesterol + O2 cholest-4-en-3-one + H2O2
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is cholesterol:oxygen oxidoreductase. Other names in common use include cholesterol- O2 oxidoreductase, 3beta-hydroxy steroid oxidoreductase, and 3beta-hydroxysteroid:oxygen oxidoreductase. This enzyme participates in bile acid biosynthesis.
The substrate-binding domain found in some bacterial cholesterol oxidases is composed of an eight-stranded mixed beta-pleated sheet and six alpha-helices. This domain is positioned over the isoalloxazine ring system of the FAD cofactor bound by the FAD-binding domain and forms the roof of the active site cavity, allowing for catalysis of oxidation and isomerisation of cholesterol to cholest-4-en-3-one.
- Richmond W (1973). "Preparation and properties of a cholesterol oxidase from Nocardia sp. and its application to the enzymatic assay of total cholesterol in serum". Clin. Chem. 19 (12): 1350–6. PMID 4757363.
- STADTMAN TC, CHERKES A, ANFINSEN CB (1954). "Studies on the microbiological degradation of cholesterol". J. Biol. Chem. 206 (2): 511–23. PMID 13143010.
|This EC 1.1 enzyme-related article is a stub. You can help Wikipedia by expanding it.|
Cholesterol oxidase, substrate-binding Provide feedback
The substrate-binding domain found in Cholesterol oxidase is composed of an eight-stranded mixed beta-pleated sheet and six alpha-helices. This domain is positioned over the isoalloxazine ring system of the FAD cofactor bound by FAD_binding_4 ( PF:PF01565) and forms the roof of the active site cavity, allowing for catalysis of oxidation and isomerisation of cholesterol to cholest-4-en-3-one .
Coulombe R, Yue KQ, Ghisla S, Vrielink A; , J Biol Chem. 2001;276:30435-30441.: Oxygen access to the active site of cholesterol oxidase through a narrow channel is gated by an Arg-Glu pair. PUBMED:11397813 EPMC:11397813
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR015213
The substrate-binding domain found in cholesterol oxidase is composed of an eight-stranded mixed beta-pleated sheet and six alpha-helices. This domain is positioned over the isoalloxazine ring system of the FAD cofactor bound by the FAD-binding domain (INTERPRO) and forms the roof of the active site cavity, allowing for catalysis of oxidation and isomerisation of cholesterol to cholest-4-en-3-one [PUBMED:11397813].
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
- the number of residues in the sequence
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This clan consists of a duplicated subdomain in a variety of FAD-liked oxidase/dehydrogenase enzymes.
The clan contains the following 6 members:ALO BBE Chol_subst-bind Cytokin-bind FAD-oxidase_C Lact-deh-memb
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
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- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the NCBI sequence database using the family HMM
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Curation and family details
|Number in seed:||3|
|Number in full:||72|
|Average length of the domain:||295.20 aa|
|Average identity of full alignment:||57 %|
|Average coverage of the sequence by the domain:||53.89 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||6|
|Download:||download the raw HMM for this family|
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There are 2 interactions for this family. More...
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Chol_subst-bind domain has been found. There are 4 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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