Substrate specificity of and product formation by muconate cycloisomerases: an analysis of wild-type enzymes and engineered variants

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Substrate specificity of and product formation by muconate cycloisomerases: an analysis of wild-type enzymes and engineered variants is …
instance of (P31):
scholarly articleQ13442814

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P932PMC publication ID106723
P698PubMed publication ID9726873

P2093author name stringA Goldman
H J Hecht
H Hoier
J Gröning
U Schell
M Schlömann
M D Vollmer
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Characterization of muconate and chloromuconate cycloisomerase from Rhodococcus erythropolis 1CP: indications for functionally convergent evolution among bacterial cycloisomerasesQ39836769
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Unusual G + C content and codon usage in catIJF, a segment of the ben-cat supra-operonic cluster in the Acinetobacter calcoaceticus chromosomeQ42602983
Chemical structure and biodegradability of halogenated aromatic compounds. Substituent effects on 1,2-dioxygenation of catecholQ42935823
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A re-evaluation of the crystal structure of chloromuconate cycloisomeraseQ47983725
Cis,cis-muconate lactonizing enzyme from Trichosporon cutaneum: evidence for a novel class of cycloisomerases in eucaryotesQ48084891
Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologousQ59012432
Rapid high-efficiency site-directed mutagenesis by the phosphorothioate approachQ67979715
The metabolism of p-fluorobenzoic acid by a Pseudomonas spQ68630317
A synthesis of protoanemonin; the tautomerism of acetylacrylic acid and of penicillic acidQ83315884
P433issue9
P407language of work or nameEnglishQ1860
P304page(s)3290-3299
P577publication date1998-09-01
P1433published inApplied and Environmental MicrobiologyQ4781593
P1476titleSubstrate specificity of and product formation by muconate cycloisomerases: an analysis of wild-type enzymes and engineered variants
P478volume64

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cites work (P2860)
Q42095985A gene cluster involved in degradation of substituted salicylates via ortho cleavage in Pseudomonas sp. strain MT1 encodes enzymes specifically adapted for transformation of 4-methylcatechol and 3-methylmuconate
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