Histidine ammonia-lyase from Streptomyces griseus

Wu, Pen-Chaur; Kroening, T A; White, Peter J; Kendrick, Kathleen E.

doi:10.1016/0378-1119(92)90535-w

Cited by 13 publications

(4 citation statements)

References 27 publications

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“…Previous studies have shown that cyanide and borohydride react with the MIO electrophile and render HAL inactive (24,26,37). A 30 min treatment with either KCN or NaBH 4 prior to the addition of substrate caused a dramatic loss of SgcC4 activity (Figure 7).…”

Section: Resultsmentioning

confidence: 85%

Kinetic Analysis of the 4-Methylideneimidazole-5-one-Containing Tyrosine Aminomutase in Enediyne Antitumor Antibiotic C-1027 Biosynthesis

et al. 2003

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The enediyne antitumor antibiotic C-1027 contains an unusual (S)-3-chloro-4,5-dihydroxy-beta-phenylalanine moiety, which requires an aminomutase for its biosynthesis. Previously, we established that SgcC4 is an aminomutase that catalyzes the conversion of L-tyrosine to (S)-beta-tyrosine and employs 4-methylideneimidazole-5-one (MIO) at its active site [Christenson, S. D., Liu, W., Toney, M. D., and Shen, B. (2003) J. Am. Chem. Soc. 125, 6062-6063]. Here, we present a thorough analysis of the properties of SgcC4. L-Tyrosine is the best substrate among those tested and most likely serves as the in vivo precursor for the (S)-3-chloro-4,5-dihydroxy-beta-phenylalanine moiety. The presence of MIO in the active site is supported by several lines of evidence. (1) Addition of ATP or divalent metal ions has no effect on its aminomutase activity. (2) SgcC4 has optimal activity at pH approximately 8.8, similar to the pH optima of MIO-dependent ammonia lyases. (3) SgcC4 is strongly inhibited by sodium borohydride and potassium cyanide, but preincubation with L-tyrosine or 4-hydroxycinnamate largely prevents this inhibition. (4) The difference spectrum between SgcC4 and its S153A mutant shows a positive peak at approximately 310 nm, indicative of MIO. (5) The S153A mutation lowers k(cat)/K(M) 640-fold. The SgcC4-catalyzed conversion of L-tyrosine to (S)-beta-tyrosine proceeds via 4-hydroxycinnamate as an intermediate. The latter also acts as a competitive inhibitor with respect to L-tyrosine and serves as an alternative substrate for the production of beta-tyrosine in the presence of an amino source. A full time course for the SgcC4-catalyzed interconversion between L-tyrosine, beta-tyrosine, and 4-hydroxycinnamate was measured and analyzed to provide estimates for the rate constants in a minimal mechanism. SgcC4 also exhibits a beta-tyrosine racemase activity, but alpha-tyrosine racemase activity was not detected.

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Section: Resultsmentioning

confidence: 85%

Kinetic Analysis of the 4-Methylideneimidazole-5-one-Containing Tyrosine Aminomutase in Enediyne Antitumor Antibiotic C-1027 Biosynthesis

et al. 2003

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“…As regards the product of hutP there was no homologous protein exhibiting significant similarity in the database (FASTA optimized score < 80). The btltH product, histidase, exhibited very high levels of homology with histidases of several organisms, including man (Suchi et al, 1993), rat (Taylor e t al., 1990), mouse (Taylor e t al., 1993), Psetldomonas ptltida (Consevage & Phillips, 1990) and Streptomyes grisetls (Wu et al, 1992), suggesting that histidase is highly conserved among evolutionarily diverse organisms. The EE57A protein showed very high homology to urocanase of P. ptltida (Fessenmaier et al, 1991).…”

Section: Genes Found In the Hut-wapa Region And Their Featuresmentioning

confidence: 99%

Cloning and sequencing of a 29 kb region of the Bacillus subtilis genome containing the hut and wapA loci

et al. 1995

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Within the framework of an international project for the sequencing of the entire Bacillus subtilis genome, a 29 kb chromosome segment, which contains the hut operon (335") and the wapA gene, has been cloned and sequenced. This region (28954 bp) contains 21 complete ORFs and one partial one. The 5th, 6th and 17th genes correspond to hutH encoding histidase, hutP encoding the positive regulator for the hut operon and wapA encoding a precursor of three major wall-associated proteins, respectively. A homology search for their products deduced from the 21 complete ORFs revealed that nine of them exhibit significant homology to known proteins such as urocanase (Pseudomonas putida), a protein involved in clavulanic acid biosynthesis (Streptomyces griseus), amino acid permeases (lysine, Escherichia coli; histidine, Saccharomyces cerewisiae; and others), figlucoside-specif ic phosphotransferases (E. coli and Erwinia chrysanthemi) and 6-phospho-& glucosidases (E. coli and Erw. chrysanthemi). Based on the features of the determined sequence and the results of the homology search, as well as on genetic data and sequence of the hut genes reported by other groups, it is predicted that the B. subtilis hut operon may consist of the following six genes (6th-lst), the last of which is followed by a typical p-independent transcription terminator: hutP, hutH, EE57A (hutU) encoding urocanase, EE57B (hut0 encoding imidazolone-5-propionate hydrolase, EE57C (hutG) encoding formiminoglutamate hydrolase and EE57D (tentatively designated as hutM) possibly encoding histidine permease. Interestingly, the direction of transcription of these hut genes is opposite to that of the movement of the replication fork.

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“…[29] Also, the HAL from Streptomyces griseus displays a CSG as MIOforming residues. [30] In most TAMs/PAMs, the classical ASG residues are present. However, bacterial PAMs with TSG as MIOforming residues have also been found.…”

Section: Introductionmentioning

confidence: 99%

“…Interestingly, the mutation of SSG back to ASG eliminated the PAL activity [29] . Also, the HAL from Streptomyces griseus displays a CSG as MIO‐forming residues [30] . In most TAMs/PAMs, the classical ASG residues are present.…”

Section: Introductionmentioning

confidence: 99%

Systematic Analysis of the MIO‐forming Residues of Aromatic Ammonia Lyases

Brack,

Sun,

et al. 2024

ChemBioChem

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Aromatic ammonia lyases (AALs) and tyrosine/phenylalanine ammonia mutases (TAM/PAM) are 3,5‐dihydro‐5‐methylidene‐4H‐imidazol‐4‐one‐ (MIO) dependent enzymes. Usually, the MIO moiety is autocatalytically formed from the tripeptide Ala‐Ser‐Gly (ASG) and acts as an electrophile during the enzymatic reaction. However, the MIO‐forming residues (ASG) have some diversity in this enzyme class. In this work, a systematic investigation on the variety of MIO‐forming residues was carried out using in‐depth sequence analyses. Several protein clusters of AAL‐like enzymes with unusual MIO‐forming residues such as ACG, TSG, SSG, and CSG were identified, including two novel histidine ammonia lyases and one PAM with CSG and TSG residues, respectively, as well as three novel ergothioneine trimethylammonia lyases without MIO motif. The mutagenesis of common MIO‐groups confirmed the function of these MIO variants, which provides good starting points for future functional prediction and mutagenesis research of AALs.

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Histidine ammonia-lyase from Streptomyces griseus

Cited by 13 publications

References 27 publications

Kinetic Analysis of the 4-Methylideneimidazole-5-one-Containing Tyrosine Aminomutase in Enediyne Antitumor Antibiotic C-1027 Biosynthesis

Kinetic Analysis of the 4-Methylideneimidazole-5-one-Containing Tyrosine Aminomutase in Enediyne Antitumor Antibiotic C-1027 Biosynthesis

Cloning and sequencing of a 29 kb region of the Bacillus subtilis genome containing the hut and wapA loci

Systematic Analysis of the MIO‐forming Residues of Aromatic Ammonia Lyases

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