1.14.11.35: 1-deoxypentalenic acid 11beta-hydroxylase

This is an abbreviated version!
For detailed information about 1-deoxypentalenic acid 11beta-hydroxylase, go to the full flat file.

Reaction

Synonyms

pntH, ptlH, sav2991

ECTree

1 Oxidoreductases

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor

1.14.11.35 1-deoxypentalenic acid 11beta-hydroxylase

Advanced search results

Do not include text mining results

Include

results (more...)

Include

results (more...)

Results	in table
91	AA Sequence
2	Cloned(Commentary)
1	Crystallization (Commentary)
1	KM Value [mM]
1	Metals/Ions
2	Molecular Weight [Da]
2	Organism
5	Pathway
1	pH Optimum
2	Protein Variants
1	Reaction
2	Reference
3	Substrates and Products (Substrate)
1	Subunits
4	Synonyms
1	Systematic Name
1	Turnover Number [1/s]

Crystallization

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Crystallization on EC 1.14.11.35 - 1-deoxypentalenic acid 11beta-hydroxylase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide

Go to Crystallization (commentary) Search

complexes with the cofactors iron, alpha-ketoglutarate, and the nonreactive enantiomer of the substrate, ent-1-deoxypentalenic acid, in four different crystal forms to up to 1.31 A resolution. The overall structure of PtlH forms a double-stranded barrel helix fold and the cofactor-binding site for iron and alpha-keto-glutarate is similar to other double-stranded barrel helix fold enzymes. Binding of the substrate enantiomer induces a reorganization of the monoclinic crystal lattice leading to a disorder-order transition of a C-terminal alpha-helix. The newly formed helix blocks the major access to the active site and effectively traps the bound substrate

Streptomyces avermitilis

Q82IZ1

719845