1992
DOI: 10.1271/bbb.56.84
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Purification and Properties of Thermostableβ-Tyrosinase from an Obligately Symbiotic Thermophile,Symbiobacterium thermophilum

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Cited by 25 publications
(4 citation statements)
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“… 33 ( Eh Tpl) and Ref. 34 ( St Tpl). *The K m values were measured at 30 ℃ for Ei Tpl and Eh Tpl and 70 ℃ for St Tpl.…”
Section: Methodsmentioning
confidence: 99%
See 1 more Smart Citation
“… 33 ( Eh Tpl) and Ref. 34 ( St Tpl). *The K m values were measured at 30 ℃ for Ei Tpl and Eh Tpl and 70 ℃ for St Tpl.…”
Section: Methodsmentioning
confidence: 99%
“…The enzymatic properties of Tpl proteins from E. intermedia ( Ei Tpl), 6 , 7 ) E. herbicola ( Eh Tpl), 33 ) and S. thermophilum ( St Tpl) 34 ) which were purified to a homogeneous state are summarized in Table 4 . The molecular masses of a single subunit of these enzymes were calculated from the amino acid sequences deduced from the nucleotide sequences.…”
Section: Properties Of Tyrosine Phenol-lyasementioning
confidence: 99%
“…Indeed, the symbiotic thermophile Symbiobacterium thermophilum, known to possess a thermostable tryptophanase, also has a similarly thermostable (optimum temperature 80 "C) tyrosine phenollyase enzyme. 92 The enzyme is a tetramer, with broad substrate specificity, degrading substrates such as S-methyl-L-cysteine and P-chloro-L-alanine to pyruvate at much higher rates than with L-tyrosine. An efficient reverse reaction synthesizing L-DOPA from catechol and pyruvate in the presence of high concentrations of ammonia was also achieved.…”
Section: Phenol and Tyrosine Phenol-lyasementioning
confidence: 99%
“…However, it is very difficult to modify the bacterium given the complexity of the L-tyrosine metabolic pathway; therefore, this method has not been widely used for industrial production. For enzymatic conversion, TPL 17,18 (EC 4.1.99.2), which is a multifunctional enzyme that requires pyridoxal phosphate (PLP), can stoichiometrically convert pyruvate, phenol, and ammonia chloride to L-tyrosine in vitro (pyruvate + phenol + ammonium chloride → L-tyrosine + H 2 O).This enzyme has been identified in many organisms, some of which exhibit increased enzyme activity, such as Citrobacter f reundii, 19 Citrobacter intermedius, 20 Erwinia herbicola, 21 Symbiobacterium thermophilum, 22 and Symbiobacterium toebii. 16,23,24 Xu 25 expressed the TPL gene from E. herbicola in Escherichia coli and produced L-tyrosine by whole-cell catalysis at 40 °C.…”
Section: ■ Introductionmentioning
confidence: 99%