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Links from Protein

Items: 7

1.

FAD-dependent monooxygenase

This domain is involved in FAD binding in a number of enzymes. [1]. 1409567. Crystal structure of the reduced form of p-hydroxybenzoate hydroxylase refined at 2.3A resolution. Schreuder HA, van der Laan JM, Swarte MB, Kalk KH, Hol WG, Drenth J;. Proteins 1992;14:178-190. (from Pfam)

GO Terms:
Molecular Function:
FAD binding (GO:0071949)
Date:
2024-10-16
Family Accession:
NF013646.5
Method:
HMM
2.
new record, indexing in progress
Family Accession:
3.
new record, indexing in progress
Family Accession:
4.

bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase

bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase catalyzes the insertion of one atom of molecular oxygen into position 2 of the phenyl ring of 3-(3-hydroxyphenyl)propionate (3-HPP) and hydroxycinnamic acid (3HCI)

Date:
2018-03-15
Family Accession:
11482118
Method:
Sparcle
5.

bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase

Date:
2021-03-12
Family Accession:
NF004831.0
Method:
HMM
6.

bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase

GO Terms:
Molecular Function:
FAD binding (GO:0071949)
Date:
2021-10-01
Family Accession:
NF004829.0
Method:
HMM
7.

bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase

GO Terms:
Molecular Function:
3-(3-hydroxyphenyl)propionate hydroxylase activity (GO:0008688)
Biological Process:
3-(3-hydroxy)phenylpropionate catabolic process (GO:0019622)
Date:
2021-10-13
Family Accession:
NF004827.0
Method:
HMM
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