Enzymes
| UniProtKB help_outline | 2 proteins |
| Enzyme class help_outline |
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- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline streptothricin F Identifier CHEBI:60822 Charge 3 Formula C19H37N8O8 InChIKeyhelp_outline NRAUADCLPJTGSF-VLSXYIQESA-Q SMILEShelp_outline [H][C@]12N\C(N[C@]1([H])C(=O)NC[C@H]2O)=[NH+]/[C@@H]1O[C@H](CO)[C@H](OC(N)=O)[C@@H](O)[C@H]1NC(=O)C[C@@H]([NH3+])CCC[NH3+] 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline streptothricin F acid Identifier CHEBI:60838 Charge 3 Formula C19H39N8O9 InChIKeyhelp_outline AJUBASUIRHJEOK-AQLSXGMYSA-Q SMILEShelp_outline [H][C@@]1(N\C(N[C@]1([H])C([O-])=O)=[NH+]/[C@@H]1O[C@H](CO)[C@H](OC(N)=O)[C@@H](O)[C@H]1NC(=O)C[C@@H]([NH3+])CCC[NH3+])[C@H](O)C[NH3+] 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:28138 | RHEA:28139 | RHEA:28140 | RHEA:28141 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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The biological function of the bacterial isochorismatase-like hydrolase SttH.
Maruyama C., Hamano Y.
The streptothricin hydrolase (SttH), which is a member of the isochorismatase-like hydrolase (ILH) super-family, catalyzes the hydrolysis of the streptolidine lactam group in streptothricin (ST) antibiotics, thereby inactivating them. In this study we identified a novel homologous gene (sttH-sn) a ... >> More
The streptothricin hydrolase (SttH), which is a member of the isochorismatase-like hydrolase (ILH) super-family, catalyzes the hydrolysis of the streptolidine lactam group in streptothricin (ST) antibiotics, thereby inactivating them. In this study we identified a novel homologous gene (sttH-sn) and sequenced the flanking regions of the sttH and sttH-sn genes. The organization of genes around the sttH, sttH-sn, and ILH genes revealed that a number of the genes were clustered with genes encoding oxidoreductases with molybdopterin binding subunits, suggesting that the true role of these gene products (SttHs and a number of ILHs) might have to do with the chemical modification of molybdopterin, rather than ST-resistance. In addition, mutant enzymes were constructed in which Ser was substituted for highly conserved Cys-176 and Cys-158 of SttH and SttH-sn respectively, and no enzyme activities were detected. Thus, biochemically, these ILHs were found to be "cysteine hydrolases." << Less
Biosci. Biotechnol. Biochem. 73:2494-2500(2009) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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A novel enzyme conferring streptothricin resistance alters the toxicity of streptothricin D from broad-spectrum to bacteria-specific.
Hamano Y., Matsuura N., Kitamura M., Takagi H.
Streptothricins (STs) produced by Streptomyces strains are broad-spectrum antibiotics. All STs consist of a carbamoylated D-gulosamine to which the beta-lysine homopolymer (1 to 7 residues) and the amide form of the unusual amino acid streptolidine (streptolidine lactam) are attached. Although man ... >> More
Streptothricins (STs) produced by Streptomyces strains are broad-spectrum antibiotics. All STs consist of a carbamoylated D-gulosamine to which the beta-lysine homopolymer (1 to 7 residues) and the amide form of the unusual amino acid streptolidine (streptolidine lactam) are attached. Although many ST-resistance genes have been identified in bacteria, including clinically isolated pathogens and ST-producing Streptomyces strains, only one resistance mechanism has been identified to date. This mechanism involves the modification of the ST molecule by monoacetylation of the moiety of the beta-lysine(s). In this study, we successfully isolated a novel ST-resistance gene (sttH) from Streptomyces albulus, which is a known ST nonproducer. The in vitro analysis of SttH demonstrated that this enzyme catalyzes the hydrolysis of the amide bond of streptolidine lactam, thereby conferring ST resistance. Interestingly, the selective toxicity of ST-D possessing 3x beta-lysine moiety was altered from broad-spectrum to bacteria-specific by the hydrolysis of streptolidine lactam, although ST-F (1 x beta-lysine) was detoxified by SttH in both prokaryotes and eukaryotes (yeasts). STs have not been clinically developed due to their toxicities; however, in this study, we showed that hydrolyzed ST-D (ST-D-acid) exhibits potent antibacterial activity even when its toxicity against eukaryotic cells is reduced by SttH. This suggests that ST-D-acid is a potential candidate for clinical development or for use as a new lead compound for drug discovery. << Less
J. Biol. Chem. 281:16842-16848(2006) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.