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Information on EC 4.2.1.145 - capreomycidine synthase
for references in articles please use BRENDA:EC4.2.1.145
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IUBMB Comments
A pyridoxal 5′-phosphate protein. The enzyme is involved in the biosynthesis of the cyclic pentapeptide antibiotic viomycin.
The enzyme appears in viruses and cellular organisms
showSynonyms
capreomycidine synthase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
VioD
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2S,3S)-3-hydroxyarginine = (2S,3R)-capreomycidine + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SYSTEMATIC NAME
IUBMB Comments
(2S,3S)-3-hydroxyarginine hydrolyase (cyclizing, (2S,3R)-capreomycidine-forming)
A pyridoxal 5'-phosphate protein. The enzyme is involved in the biosynthesis of the cyclic pentapeptide antibiotic viomycin.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2S,3S)-3-hydroxyarginine
(2S,3R)-capreomycidine
-
Substrates: -
Products: -
Products: -
?
(2S,3S)-3-hydroxyarginine
(2S,3R)-capreomycidine
-
Substrates: -
Products: -
Products: -
?
(2S,3S)-3-hydroxyarginine
(2S,3R)-capreomycidine
-
Substrates: the enzyme is involved in the biosynthesis of the cyclic pentapeptide antibiotic viomycin
Products: -
Products: -
?
(2S,3S)-3-hydroxyarginine
(2S,3R)-capreomycidine
-
Substrates: the enzyme catalyzes an intramolecular beta-replacement/elimination reaction. VioD is completely stereospecific for (3S)-hydroxy-L-Arg, as no product formation is observed when (3R)-hydroxy-L-Arg is evaluated as substrate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2S,3S)-3-hydroxyarginine
(2S,3R)-capreomycidine
-
Substrates: -
Products: -
Products: -
?
(2S,3S)-3-hydroxyarginine
(2S,3R)-capreomycidine
-
Substrates: -
Products: -
Products: -
?
(2S,3S)-3-hydroxyarginine
(2S,3R)-capreomycidine
-
Substrates: the enzyme is involved in the biosynthesis of the cyclic pentapeptide antibiotic viomycin
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate dependent enzyme. It is not known if the cofactor is covalently bound to VioD through a lysyl imine, as is common with many PLP-dependent enzymes
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
the enzyme is involved in the biosynthesis of the cyclic pentapeptide antibiotic viomycin
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A644XJP3_9ZZZZ
374
0
43132
TrEMBL
other Location (Reliability: 1)
A0A2R8BCA6_9RHOB
379
0
42370
TrEMBL
-
A0A644SSX0_9ZZZZ
399
0
45368
TrEMBL
other Location (Reliability: 4)
A0A645A945_9ZZZZ
247
0
27753
TrEMBL
other Location (Reliability: 2)
A0A644TIV2_9ZZZZ
391
0
43165
TrEMBL
other Location (Reliability: 2)
A0A644YKB8_9ZZZZ
277
0
30796
TrEMBL
other Location (Reliability: 1)
A0A644VVN5_9ZZZZ
368
0
41600
TrEMBL
other Location (Reliability: 4)
A0A645AM50_9ZZZZ
417
1
47284
TrEMBL
other Location (Reliability: 5)
A0A645FQE0_9ZZZZ
209
0
24056
TrEMBL
other Location (Reliability: 2)
A0A8J7AD46_9CYAN
378
0
42407
TrEMBL
-
A0A6J5FAH4_9BURK
399
0
43303
TrEMBL
-
A0A645DV62_9ZZZZ
231
0
25687
TrEMBL
Mitochondrion (Reliability: 5)
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned into the Escherichia coli expression vector pET28a encoding a N-terminal His6-tag
-
overproduced in Escherichia coli with an N-terminal hexahistidine affinity tag
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yin, X.; McPhail, K.L., Kim, K.J.; Zabriskie, T.M.
Formation of the nonproteinogenic amino acid 2S,3R-capreomycidine by VioD from the viomycin biosynthesis pathway
Chembiochem
5
1278-1281
2004
Streptomyces vinaceus
brenda
Ju, J.; Ozanick, S.G.; Shen, B.; Thomas, M.,G.
Conversion of (2S)-arginine to (2S,3R)-capreomycidine by VioC and VioD from the viomycin biosynthetic pathway of Streptomyces sp. strain ATCC11861
Chembiochem
5
1281-1285
2004
Streptomyces sp., Streptomyces sp. ATCC 11861
brenda
EXTERNAL LINKS (specific for EC-Number 4.2.1.145)
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Release 2023.1 (January 2023)
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