2.7.7.47: streptomycin 3''-adenylyltransferase
This is an abbreviated version!
For detailed information about streptomycin 3''-adenylyltransferase, go to the full flat file.
Word Map on EC 2.7.7.47
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2.7.7.47
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integrons
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medicine
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aminoglycoside-modifying
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blavim-2
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streptomycin-resistant
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dfra15
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diagnostics
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agriculture
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analysis
- 2.7.7.47
- integrons
- medicine
-
aminoglycoside-modifying
- blavim-2
-
streptomycin-resistant
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dfra15
- diagnostics
- agriculture
- analysis
Reaction
Synonyms
AAD (3''), aadA, AadA6, aminoglycoside (3'')(9) adenylyltransferase, aminoglycoside 3''-adenylyltransferase, aminoglycoside 3'-adenyltransferase, aminoglycoside adenyltransferase, aminoglycoside adenyltransferase A, aminoglycoside adenyltransferase type A, aminoglycoside adenylyltransferase, ANT(3'')-II, ANT(3'')-Ii/AAC(6')-IId, SMATase, str, streptomycin adenylate synthetase, streptomycin adenyltransferase, streptomycin adenylylase, streptomycin adenylyltransferase, streptomycin-spectinomycin adenylyltransferase
ECTree
2.7.7.47 streptomycin 3''-adenylyltransferaseAdvanced search results
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results (Engineering
Engineering on EC 2.7.7.47 - streptomycin 3''-adenylyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D178A
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the mutation destabilizes the enzyme leading to reduced melting temperature (47 C). When titrated with streptomycin, temperature stabilization occurs at higher streptomycin concentration compared with wild type, indicating weaker binding affinity
E87Q
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the nonadenylating mutant can hydrolyze ATP in the presence of streptomycin. The mutant does not convey resistance to streptomycin but still binds ATP and streptomycin, although with 4 and 20fold lower affinity than the wild type enzyme
W173A
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the mutation destabilizes the enzyme leading to reduced melting temperature (50 C). When titrated with streptomycin, temperature stabilization occurs at higher streptomycin concentration compared with wild type, indicating weaker binding affinity
D182A
mutation reduces the MIC of streptomycin and spectinomycin
D182N
mutation reduces the MIC of streptomycin and spectinomycin
E87A
mutation reduces the MIC of streptomycin and spectinomycin to that of an AadA null strain
E87Q
mutation reduces the MIC of streptomycin and spectinomycin to that of an AadA null strain
K205A
mutation reduces the MIC of streptomycin and spectinomycin
R192A
mutation reduces the MIC of streptomycin and spectinomycin
W112A
mutation reduces the MIC of spectinomycin to that of an AadA null strain and reduces the MIC of streptomycin
W112F
mutation reduces the MIC of spectinomycin to that of an AadA null strain and reduces the MIC of streptomycin
additional information
additional information
amino acid sequence of str is 80.3% and 13.9% identical to 6'-streptomycin adenylyltransferase (aadE) and 3'-streptomycin adenylyltransferase (aadA), respectively, from Enterococcus
additional information
amino acid sequence shows 100% identity to plasmid-mediated streptomycin adenylyltransferase gene from Lactococcus lactis
additional information
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amino acid sequence of str is 80.3% and 13.9% identical to 6'-streptomycin adenylyltransferase (aadE) and 3'-streptomycin adenylyltransferase (aadA), respectively, from Enterococcus
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additional information
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amino acid sequence shows 100% identity to plasmid-mediated streptomycin adenylyltransferase gene from Lactococcus lactis
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additional information
generation of a carboxy-terminal truncated variant molecule, residues 1-264. The truncated residues have little influence on protein folding, whereas they have a positive effect on the enzymic activity and stabilize dimers at high protein concentrations
additional information
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generation of a carboxy-terminal truncated variant molecule, residues 1-264. The truncated residues have little influence on protein folding, whereas they have a positive effect on the enzymic activity and stabilize dimers at high protein concentrations
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