Information on EC 1.14.19.B8 - [peptidyl-carrier-protein SgcC2]-(3S)-beta-tyrosyl thioester 3-halogenase

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The expected taxonomic range for this enzyme is: Streptomyces globisporus

EC NUMBER
COMMENTARY hide
1.14.19.B8
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
[peptidyl-carrier-protein SgcC2]-(3S)-beta-tyrosyl thioester 3-halogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-(3S)-beta-tyrosyl-[peptidyl-carrier-protein SgcC2]-L-cysteine + FADH2 + Cl- + O2 + H+ = S-(S3)-3-chloro-beta-tyrosyl-[peptidyl-carrier-protein SgcC2]-L-cysteine + FAD + 2 H2O
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
S-(3S)-beta-tyrosyl-[peptidyl-carrier-protein SgcC2]-L-cysteine:FADH2 oxidoreductase (3-halogenating)
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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the enzyme is involved in the biosynthesis of the (S)-3-chloro-5-hydroxy-beta-tyrosine moiety prior to incorporation into the chromoprotein antitumor antibiotic C-1027
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-(3R)-beta-tyrosyl-[peptidyl-carrier-protein SgcC2]-L-cysteine + 2 FADH2 + 2 H+ + Cl- + O2
S-(3R)-3-chloro-beta-tyrosyl-[peptidyl-carrier-protein SgcC2]-L-cysteine + FAD + 2 H2O
show the reaction diagram
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-
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?
S-(3S)-beta-tyrosyl-[peptidyl-carrier-protein SgcC2]-L-cysteine + 2 FADH2 + 2 H+ + Br- + O2
S-(3S)-3-bromo-beta-tyrosyl-[peptidyl-carrier-protein SgcC2]-L-cysteine + FAD + 2 H2O
show the reaction diagram
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the enzyme can also efficiently catalyzes bromination but not fluorination or iodination
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?
S-(3S)-beta-tyrosyl-[peptidyl-carrier-protein SgcC2]-L-cysteine + 2 FADH2 + 2 H+ + Cl- + O2
S-(3S)-3-chloro-beta-tyrosyl-[peptidyl-carrier-protein SgcC2]-L-cysteine + FAD + 2 H2O
show the reaction diagram
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-
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-
?
S-(3S)-beta-tyrosyl-[peptidyl-carrier-protein SgcC2]-L-cysteine + 2 FADH2 + 2 H+ + Cl- + O2
S-(S3)-3-chloro-beta-tyrosyl-[peptidyl-carrier-protein SgcC2]-L-cysteine + FAD + 2 H2O
show the reaction diagram
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the enzyme is involved in the biosynthesis of the (S)-3-chloro-5-hydroxy-beta-tyrosine moiety prior to incorporation into the chromoprotein antitumor antibiotic C-1027
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-
?
additional information
?
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the enzyme does not catalyze fluorination or iodination. The enzyme can not utilize 3-hydroxy-beta-tyrosyl-S-SgcC2 as a substrate
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-(3S)-beta-tyrosyl-[peptidyl-carrier-protein SgcC2]-L-cysteine + 2 FADH2 + 2 H+ + Cl- + O2
S-(S3)-3-chloro-beta-tyrosyl-[peptidyl-carrier-protein SgcC2]-L-cysteine + FAD + 2 H2O
show the reaction diagram
-
the enzyme is involved in the biosynthesis of the (S)-3-chloro-5-hydroxy-beta-tyrosine moiety prior to incorporation into the chromoprotein antitumor antibiotic C-1027
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-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7.5
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pH 5.5: about 15% of maximal activity, pH 7.5: about 65% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE