1.14.11.21: clavaminate synthase
This is an abbreviated version!
For detailed information about clavaminate synthase, go to the full flat file.
Word Map on EC 1.14.11.21
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1.14.11.21
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clavulanic
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clavuligerus
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alpha-ketoglutarate
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proclavaminic
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beta-lactamase
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dioxygenase
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non-heme
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cs2
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oxygenases
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clavams
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dioxygen
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alpha-ketoglutarate-dependent
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desaturation
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amidinohydrolase
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2-his-1-carboxylate
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synthesis
- 1.14.11.21
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clavulanic
- clavuligerus
- alpha-ketoglutarate
-
proclavaminic
- beta-lactamase
- dioxygenase
-
non-heme
- cs2
- oxygenases
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clavams
- dioxygen
-
alpha-ketoglutarate-dependent
-
desaturation
-
amidinohydrolase
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2-his-1-carboxylate
- synthesis
Reaction
Synonyms
CAS, CAS1, CAS2, clavaminate synthase 1, clavaminate synthase 2, clavaminic acid synthase, CS, synthase, clavaminate
ECTree
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Engineering
Engineering on EC 1.14.11.21 - clavaminate synthase
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C162L
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isozyme CAS2, site-directed mutagenesis, same activity in hydroxylation of N-alpha-acetyl-L-arginine as the wild-type enzyme
C200L
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isozyme CAS2, site-directed mutagenesis, 42% activity in hydroxylation of N-alpha-acetyl-L-arginine compared to the wild-type enzyme
C201L
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isozyme CAS2, site-directed mutagenesis, 40% activity in hydroxylation of N-alpha-acetyl-L-arginine compared to the wild-type enzyme
C8L
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isozyme CAS2, site-directed mutagenesis, 42% activity in hydroxylation of N-alpha-acetyl-L-arginine compared to the wild-type enzyme
H109L
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isozyme CAS2, site-directed mutagenesis, 86% activity in hydroxylation of N-alpha-acetyl-L-arginine compared to the wild-type enzyme
H109Q
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isozyme CS2, site-directed mutagensis, 83% activity of clavaminate formation compared to the wild-type enzyme, unaltered hydroxylating activity
H122L
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isozyme CAS2, site-directed mutagenesis, below 1% activity in hydroxylation of N-alpha-acetyl-L-arginine compared to the wild-type enzyme
H122Q
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isozyme CS2, site-directed mutagensis, 96% activity of clavaminate formation compared to the wild-type enzyme, unaltered hydroxylating activity
H131L
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isozyme CAS2, site-directed mutagenesis, 36% activity in hydroxylation of N-alpha-acetyl-L-arginine compared to the wild-type enzyme
H131Q
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isozyme CS2, site-directed mutagensis, 16% activity of clavaminate formation compared to the wild-type enzyme, unaltered hydroxylating activity
H145E
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isozyme CAS2, site-directed mutagenesis, below 1% activity in hydroxylation of N-alpha-acetyl-L-arginine compared to the wild-type enzyme
H145L
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isozyme CAS2, site-directed mutagenesis, below 1% activity in hydroxylation of N-alpha-acetyl-L-arginine compared to the wild-type enzyme
H145Q
H151l
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isozyme CAS2, site-directed mutagenesis, below 1% activity in hydroxylation of N-alpha-acetyl-L-arginine compared to the wild-type enzyme
H151Q
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isozyme CS2, site-directed mutagensis, 10% activity of clavaminate formation compared to the wild-type enzyme, unaltered hydroxylating activity
H167L
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isozyme CAS2, site-directed mutagenesis, 19% activity in hydroxylation of N-alpha-acetyl-L-arginine compared to the wild-type enzyme
H167Q
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isozyme CS2, site-directed mutagensis, 95% activity of clavaminate formation compared to the wild-type enzyme, unaltered hydroxylating activity
H280L
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isozyme CAS2, site-directed mutagenesis, 86% activity in hydroxylation of N-alpha-acetyl-L-arginine compared to the wild-type enzyme
H280Q
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isozyme CS2, site-directed mutagensis, no activity of clavaminate formation, but slight hydroxylating activity of deoxyguanidinoproclavaminate
H297L
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isozyme CAS2, site-directed mutagenesis, 3% activity in hydroxylation of N-alpha-acetyl-L-arginine compared to the wild-type enzyme
H297Q
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isozyme CS2, site-directed mutagensis, 65% activity of clavaminate formation compared to the wild-type enzyme, unaltered hydroxylating activity
Q154L
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isozyme CAS2, site-directed mutagenesis, 23% activity in hydroxylation of N-alpha-acetyl-L-arginine compared to the wild-type enzyme
additional information
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isozyme CS2, site-directed mutagensis, no activity of clavaminate formation, but slight hydroxylating activity of deoxyguanidinoproclavaminate
H145Q
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site-directed mutagenesis, no activity in hydroxylation of N-alpha-acetyl-L-arginine
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construction of a disruption mutant of isozyme cas2 by a gene replacement procedure, mutant shows no activity in starch-asparagine medium, but reduced activity, compared to the wild-type, in soy medium which is due to CAS1 isozyme, different regulation of the 2 isozymes concerning nutritional conditions
additional information
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construction of a disruption mutant of isozyme cas2 by a gene replacement procedure, mutant shows no activity in starch-asparagine medium, but reduced activity, compared to the wild-type, in soy medium which is due to CAS1 isozyme, different regulation of the 2 isozymes concerning nutritional conditions
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