5.4.3.2: lysine 2,3-aminomutase
This is an abbreviated version!
For detailed information about lysine 2,3-aminomutase, go to the full flat file.
Word Map on EC 5.4.3.2
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5.4.3.2
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s-adenosylmethionine
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5\'-deoxyadenosyl
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epr
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pyridoxal
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l-beta-lysine
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hyperfine
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adenosylcobalamin-dependent
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formate-lyase
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subterminale
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aldimine
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pyridoxal-5'-phosphate
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adenosylcobalamin
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5'-deoxyadenosine
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cxxxcxxc
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homolytic
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deoxyadenosyl
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aminomutases
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synthesis
- 5.4.3.2
- s-adenosylmethionine
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5\'-deoxyadenosyl
- epr
- pyridoxal
- l-beta-lysine
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hyperfine
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adenosylcobalamin-dependent
- formate-lyase
- subterminale
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aldimine
- pyridoxal-5'-phosphate
- adenosylcobalamin
- 5'-deoxyadenosine
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cxxxcxxc
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homolytic
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deoxyadenosyl
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aminomutases
- synthesis
Reaction
Synonyms
AblA, Aminomutase, lysine 2,3-, HD73_2540, KAM, kamA, L-Lysine-2,3-aminomutase, LAM, lysine 2,3-aminomutase, lysine-2,3-aminomutase, Mutase, lysine 2,3-amino-, YjeK
ECTree
Advanced search results
Engineering
Engineering on EC 5.4.3.2 - lysine 2,3-aminomutase
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D165N
about 0.1% of wild-type activity, 0.23 mol iron and 0.13 mol sulfur per mol of subunit
D172N
no catalytic activity, 0.43 mol iron and 0.13 mol sulfur per mol of subunit
D293N
no catalytic activity, 0.97 mol iron and 0.05 mol sulfur per mol of subunit. Involved in binding of epsilon-aminium and alpha-carboxylate groups of substrate
D330A
no catalytic activity, 1.9 mol iron and 1.3 mol sulfur per mol of subunit. Involved in binding of epsilon-aminium and alpha-carboxylate groups of substrate
D330N
no catalytic activity, 1.0 mol iron and 0.63 mol sulfur per mol of subunit
D96N
less than 1% of wild-type activity, 1.2 mol iron and 0.95 mol sulfur per mol of subunit
E236Q
about 1% of wild-type activity, 0.7 mol iron and 0.5 mol sulfur per mol of subunit
E86Q
about 20% of wild-type activity, 0.5 mol iron and 0.4 mol sulfur per mol of subunit
R130K
no catalytic activity, 0.2 mol iron and 0.3 mol sulfur per mol of subunit
R130Q
no catalytic activity, 0.42 mol iron and 0.2 mol sulfur per mol of subunit
R134K
no catalytic activity, 1.5 mol iron and 1.5 mol sulfur per mol of subunit
R134Q
no catalytic activity, 2.8 mol iron and 2.7 mol sulfur per mol of subunit. Involved in binding of epsilon-aminium and alpha-carboxylate groups of substrate
R135K
about 16% of wild-type activity, 2.4 mol iron and 1.6 mol sulfur per mol of subunit
R135Q
about 1.5% of wild-type activity, 1.8 mol iron and 1.5 mol sulfur per mol of subunit
R136Q
about 1.2% of wild-type activity, 0.48 mol iron and 0.35 mol sulfur per mol of subunit
D165N
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about 0.1% of wild-type activity, 0.23 mol iron and 0.13 mol sulfur per mol of subunit
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D172N
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no catalytic activity, 0.43 mol iron and 0.13 mol sulfur per mol of subunit
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D293N
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no catalytic activity, 0.97 mol iron and 0.05 mol sulfur per mol of subunit. Involved in binding of epsilon-aminium and alpha-carboxylate groups of substrate
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D96N
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less than 1% of wild-type activity, 1.2 mol iron and 0.95 mol sulfur per mol of subunit
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R134Q
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no catalytic activity, 2.8 mol iron and 2.7 mol sulfur per mol of subunit. Involved in binding of epsilon-aminium and alpha-carboxylate groups of substrate
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DELTAabl::pac
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deletion mutant, loss of the ability to synthesise Nepsilon-acetyl-beta-lysine
additional information
generation of kamR and kamA mutants by homologous recombination to examine the role of the kam locus. The results show that the sporulation rate in Bacillus thuringiensis mutant strain HD (DELTAkamR) is slightly decreased compared to that in wild-type strain HD73, whereas that in strain HD (DELTAkamA) it is similar to that in strain HD73. Other genes regulated by KamR are important for sporulation. Construction of yodT and kamA promoter fusions with lacZ
additional information
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generation of kamR and kamA mutants by homologous recombination to examine the role of the kam locus. The results show that the sporulation rate in Bacillus thuringiensis mutant strain HD (DELTAkamR) is slightly decreased compared to that in wild-type strain HD73, whereas that in strain HD (DELTAkamA) it is similar to that in strain HD73. Other genes regulated by KamR are important for sporulation. Construction of yodT and kamA promoter fusions with lacZ
additional information
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generation of kamR and kamA mutants by homologous recombination to examine the role of the kam locus. The results show that the sporulation rate in Bacillus thuringiensis mutant strain HD (DELTAkamR) is slightly decreased compared to that in wild-type strain HD73, whereas that in strain HD (DELTAkamA) it is similar to that in strain HD73. Other genes regulated by KamR are important for sporulation. Construction of yodT and kamA promoter fusions with lacZ
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additional information
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enzyme knockout mutant generation, phenotype, overview
additional information
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enzyme knockout mutant generation, phenotype, overview
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