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Information on EC 3.5.2.19 - streptothricin hydrolase
for references in articles please use BRENDA:EC3.5.2.19
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EC Tree 3 Hydrolases
3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
3.5.2 In cyclic amides
3.5.2.19 streptothricin hydrolase
IUBMB Comments
The enzyme also catalyses the hydrolysis of streptothricin-D to streptothricin-D acid . The enzyme is responsible for streptothricin resistance in Streptomyces albulus and Streptomyces noursei [1,2].
The enzyme appears in viruses and cellular organisms
showSynonyms
streptothricin hydrolase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
sstH
sttH
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
streptothricin-F + H2O = streptothricin-F acid
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
streptothricin-F hydrolase
The enzyme also catalyses the hydrolysis of streptothricin-D to streptothricin-D acid [1]. The enzyme is responsible for streptothricin resistance in Streptomyces albulus and Streptomyces noursei [1,2].
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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
streptothricin-D + H2O
streptothricin-D acid
Substrates: -
Products: -
Products: -
?
streptothricin-D + H2O
streptothricin-D acid
Substrates: -
Products: the product is identified by reverse-phase HPLC
Products: the product is identified by reverse-phase HPLC
?
streptothricin-D + H2O
streptothricin-D acid
Substrates: -
Products: the product is identified by reverse-phase HPLC
Products: the product is identified by reverse-phase HPLC
?
streptothricin-D + H2O
streptothricin-D acid
Streptomyces noursei NBRC 14147
Substrates: -
Products: the product is identified by reverse-phase HPLC
Products: the product is identified by reverse-phase HPLC
?
streptothricin-D + H2O
streptothricin-D acid
Streptomyces noursei NBRC14147
-
Substrates: -
Products: the product is identified by reverse-phase HPLC
Products: the product is identified by reverse-phase HPLC
?
streptothricin-D + H2O
streptothricin-D acid
Substrates: -
Products: -
Products: -
?
streptothricin-D + H2O
streptothricin-D acid
Substrates: -
Products: the product is identified by reverse-phase HPLC
Products: the product is identified by reverse-phase HPLC
?
streptothricin-F + H2O
streptothricin-F acid
Substrates: -
Products: -
Products: -
?
streptothricin-F + H2O
streptothricin-F acid
Substrates: -
Products: the product is identified by reverse-phase HPLC
Products: the product is identified by reverse-phase HPLC
?
streptothricin-F + H2O
streptothricin-F acid
Substrates: -
Products: the product is identified by reverse-phase HPLC
Products: the product is identified by reverse-phase HPLC
?
streptothricin-F + H2O
streptothricin-F acid
Streptomyces noursei NBRC 14147
Substrates: -
Products: the product is identified by reverse-phase HPLC
Products: the product is identified by reverse-phase HPLC
?
streptothricin-F + H2O
streptothricin-F acid
Streptomyces noursei NBRC14147
-
Substrates: -
Products: the product is identified by reverse-phase HPLC
Products: the product is identified by reverse-phase HPLC
?
streptothricin-F + H2O
streptothricin-F acid
Substrates: -
Products: -
Products: -
?
streptothricin-F + H2O
streptothricin-F acid
Substrates: -
Products: the product is identified by reverse-phase HPLC
Products: the product is identified by reverse-phase HPLC
?
additional information
?
-
Substrates: the true role of SttH may not be its involvement in resistance against streptothricins, instead, it may catalyze the hydrolysis of naturally occurring cyclic amide compounds in the metabolism of Streptomyces albulus
Products: -
Products: -
?
additional information
?
-
Substrates: this enzyme catalyzes the hydrolysis of the amide bond of streptolidine lactam, thereby conferring streptothricin resistance
Products: -
Products: -
?
additional information
?
-
Streptomyces noursei NBRC14147
Substrates: the true role of SttH may not be its involvement in resistance against streptothricins, instead, it may catalyze the hydrolysis of naturally occurring cyclic amide compounds in the metabolism of Streptomyces albulus
Products: -
Products: -
?
additional information
?
-
Streptomyces noursei NBRC14147
Substrates: this enzyme catalyzes the hydrolysis of the amide bond of streptolidine lactam, thereby conferring streptothricin resistance
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
streptothricin-D + H2O
streptothricin-D acid
Substrates: -
Products: -
Products: -
?
streptothricin-D + H2O
streptothricin-D acid
Substrates: -
Products: -
Products: -
?
streptothricin-F + H2O
streptothricin-F acid
Substrates: -
Products: -
Products: -
?
streptothricin-F + H2O
streptothricin-F acid
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: the true role of SttH may not be its involvement in resistance against streptothricins, instead, it may catalyze the hydrolysis of naturally occurring cyclic amide compounds in the metabolism of Streptomyces albulus
Products: -
Products: -
?
additional information
?
-
Streptomyces noursei NBRC14147
Substrates: the true role of SttH may not be its involvement in resistance against streptothricins, instead, it may catalyze the hydrolysis of naturally occurring cyclic amide compounds in the metabolism of Streptomyces albulus
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45 - 65
45°C: maximal activity, 65°C: about 90% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Streptomyces noursei NBRC14147
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
malfunction
physiological function
malfunction
construction of an sttH gene-knockout mutant. The minimum inhibitory concentration MIC of Streptothricins in the sttH gene-knockout mutant is determined to be 6.25 mg/ml, whereas the MIC of streptothricins in the Streptomyces albulus wild strain is determined to be above 400 mg/ml. This result clearly demonstrate that sttH is the sole gene responsible for streptothricin resistance in the Streptomyces albulus strain
malfunction
Streptomyces noursei NBRC14147
-
construction of an sttH gene-knockout mutant. The minimum inhibitory concentration MIC of Streptothricins in the sttH gene-knockout mutant is determined to be 6.25 mg/ml, whereas the MIC of streptothricins in the Streptomyces albulus wild strain is determined to be above 400 mg/ml. This result clearly demonstrate that sttH is the sole gene responsible for streptothricin resistance in the Streptomyces albulus strain
-
physiological function
sttH gene is not essential for growth. The true role of SttH may not be its involvement in resistance against streptothricins, instead, it may catalyze the hydrolysis of naturally occurring cyclic amide compounds in the metabolism of Streptomyces albulus
physiological function
Streptomyces noursei NBRC14147
-
sttH gene is not essential for growth. The true role of SttH may not be its involvement in resistance against streptothricins, instead, it may catalyze the hydrolysis of naturally occurring cyclic amide compounds in the metabolism of Streptomyces albulus
-
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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). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C176S
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Maruyama, C.; Hamano, Y.
The biological function of the bacterial isochorismatase-like hydrolase SttH
Biosci. Biotechnol. Biochem.
73
2494-2500
2009
Streptomyces noursei, Streptomyces noursei (C5NU54), Streptomyces noursei NBRC14147, Streptomyces noursei NBRC15452 (C5NU54)
brenda
Hamano, Y.; Matsuura, N.; Kitamura, M.; Takagi, H.
A novel enzyme conferring streptothricin resistance alters the toxicity of streptothricin D from broad-spectrum to bacteria-specific
J. Biol. Chem.
281
16842-16848
2006
Streptomyces noursei (Q1MW86), Streptomyces noursei NBRC 14147 (Q1MW86)
brenda
Hamano, Y.; Maruyama, C.; Kimoto, H.
Construction of a knockout mutant of the Streptothricin-resistance gene in Streptomyces albulus by electroporation
Actinomycetologica
20
35-41
2006
Streptomyces noursei (Q1MW86), Streptomyces noursei NBRC14147 (Q1MW86)
-
brenda
EXTERNAL LINKS (specific for EC-Number 3.5.2.19)
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Release 2026.1 (March 2026)
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