EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
  1.14.14.15 | (3S)-3-amino-3-(3-chloro-4-hydroxyphenyl)propanoyl-[peptidyl-carrier protein SgcC2] + FADH2 + O2 |
- |
Streptomyces globisporus |
(3S)-3-amino-3-(3-chloro-4,5-dihydroxyphenyl)propanoyl-[peptidyl-carrier protein SgcC2] + FAD + H2O |
- |
? |
| 1.14.14.15 | (R)-alpha-tyrosyl-[SgcC2] + FADH2 + O2 |
SgcC3 can utilize both (S)- and (R)-alpha-tyrosyl-[SgcC2] but not 3-hydroxy-alpha-tyrosyl-[SgcC2] as a substrate |
Streptomyces globisporus |
? |
- |
? |
| 1.14.14.15 | (S)-alpha-tyrosyl-[SgcC2] + FADH2 + O2 |
SgcC3 can utilize both (S)- and (R)-alpha-tyrosyl-[SgcC2] but not 3-hydroxy-alpha-tyrosyl-[SgcC2] as a substrate |
Streptomyces globisporus |
? |
- |
? |
| 1.14.14.15 | beta-aminoacyl-S-SgcC + FADH2 + O2 |
- |
Streptomyces globisporus |
? |
- |
? |
| 1.14.14.15 | more |
no activity with [peptidyl-carrier-protein SgcC2]-beta-tyrosyl thioester and [peptidyl-carrier-protein SgcC2]-(S)-3-hydroxy-beta-tyrosyl thioester |
Streptomyces globisporus |
? |
- |
? |
| 1.14.14.15 | more |
SgcC3 also efficiently catalyzes bromination but not fluorination or iodination |
Streptomyces globisporus |
? |
- |
? |
| 1.14.14.15 | more |
no activity with 3-hydroxy-alpha-tyrosyl-S-SgcC2 |
Streptomyces globisporus |
? |
- |
? |
| 1.14.14.15 | more |
subunit SgcE6 is responsible for the production of FADH2. FADH2 diffuses to SgcC, where Arg119 activates an O2 molecule to form a C-4a-hydroperoxyflavin intermediate. SgcC2 interacts with SgcC and guides the (S)-3-chloro-beta-tyrosyl moiety into the active site. It is activated by conserved general base His161, which results in electrophilic attack of the hydroxy group of the C-4a-hydroperoxyflavin intermediate, introducing a hydroxy group at the C-5 position of the (S)-3-chloro-beta-tyrosyl moiety. The hydroxyflavin (FADHO-) abstracts a proton from the C-5 atom of the intermediate, resulting in the formation of the rearomatizated (S)-3-chloro-5-hydroxy-beta-tyrosyl-S-SgcC2, which then dissociates from SgcC. Finally, the hydroxyflavin (FADHOH) undergoes dehydration to form FAD, which is released and recycled by SgcE6 |
Streptomyces globisporus |
? |
- |
? |
| 1.14.14.15 | S-((3S)-3-amino-3-(3-bromo-4-hydroxyphenyl)propanoyl)-[peptidyl-carrier protein SgcC2] + FADH2 + O2 |
- |
Streptomyces globisporus |
S-((3S)-3-amino-3-(3-bromo-4,5-dihydroxyphenyl)propanoyl)-[peptidyl-carrier protein SgcC2] + FAD + H2O |
- |
? |
| 1.14.14.15 | S-((3S)-3-amino-3-(3-chloro-4-hydroxyphenyl)propanoyl)-[peptidyl-carrier protein SgcC2] + FADH2 + O2 |
- |
Streptomyces globisporus |
S-((3S)-3-amino-3-(3-chloro-4,5-dihydroxyphenyl)propanoyl)-[peptidyl-carrier protein SgcC2] + FAD + H2O |
- |
? |
