Amino acid sequence of a peptide containing the active cysteine residue of histidine ammonia-lyase

Hassall, H.; Soutar, Anne K.

doi:10.1042/bj1370559

Cited by 14 publications

(15 citation statements)

References 25 publications

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“…Earlier studies on histidases from P. acidovorans ATCC 11299b by Klee and Gladner (14) and P. testosteroni NCIB 10808 by Hassall and Soutar (11) reported that the native tetramer form of these proteins could be modified by iodo[14C]acetate, from which a labeled tryptic peptide could be isolated and characterized. Whereas only the composition was reported by Klee and Gladner (14), Hassall and Soutar (11) determined its sequence to be Gly-Leu-Leu-Asp-GlySer-Ala-Ile-Asn-Pro-Ser-His-Pro-Asn-CMCys-Gly-Arg.…”

Section: Discussionmentioning

confidence: 99%

Sequence analysis of the hutH gene encoding histidine ammonia-lyase in Pseudomonas putida

Consevage

Phillips

1990

J Bacteriol

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The complete nucleotide sequence of the hutH gene, encoding histidine ammonia-lyase (histidase), in Pseudomonas putida ATCC 12633 has been determined from the appropriate portions of the hut region that had been cloned into Escherichia coli. The resulting DNA sequence revealed an open reading frame of 1,530 base pairs, corresponding to a protein subunit of approxinate molecular weight 53,600, in the location previously identified for the histidase gene by TnlO00 mutagenesis. Translation began at a GTG codon, but direct protein sequencing revealed that the initiating amino acid was removed posttranslationally to provide an N-terminal threonine; 11 additional residues completely agreed with the predicted amino acid sequence. This sequence excluded the possibility that a dehydroalanine unit, the postulated coenzyme for histidase, is attached at the N terminus of histidase subunits. Comparison of the P. putida histidase gene sequence with that of a Bacillus subtiUs region encoding histidase revealed 42% identity at the protein level. Although the hutU (urocanase) and hutH (histidase) genes are induced by urocanate and normally are transcribed as a unit beginning with hutU, analysis of the region immediately upstream of the histidase gene revealed a potential weak promoter that may possibly be used to maintain a basal level of histidase for the generation of inducer (urocanate) when histidine levels are elevated.Histidine ammonia-lyase (histidase; EC 4.3.1.3) from Pseudomonas putida possesses an essential electrophilic center whose properties are consistent with its tentative identification as a dehydroalanine (DHA) unit (5). This conclusion is based on the chromatographic detection of [3H]alanine from acid hydrolysates of histidase that had been inactivated by reduction with NaB3H4 and a similar identification of ['4C]aspartate from acid-hydrolyzed enzyme that had been treated with Na'4CN. Analogous findings have been obtained for the histidase from Pseudomonas acidovorans ATCC 11299b (9, 31). Little is known regarding the possible mechanistic involvement of DHA in the action of the enzyme or the nature of its binding to the protein.We have previously shown (5) that P. putida histidase is a tetramer with identical subunits of molecular weight approximately 55,000 and 4 mol of DHA per mol of tetrameric protein, although total activity is lost upon covalent modification of one of the DHA units. It was also found that DHA residues are present in the native unpurified enzyme, thereby indicating that they do not arise by 1B elimination of a carbohydrate or similar moiety during the purification process (5). Furthermore, Givot and Abeles inactivated rat liver histidase in vivo by modification of its electrophilic center with nitromethane and demonstrated that the products formed were the same as those found with the P. acidovorans enzyme (8).The structural gene for histidase, along with genes for the other enzymes and major control elements of histidine utilization (hut) in P. putida, has been cloned into Escherichia coli...

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Section: Discussionmentioning

confidence: 99%

Sequence analysis of the hutH gene encoding histidine ammonia-lyase in Pseudomonas putida

Consevage

Phillips

1990

J Bacteriol

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“…The organism was subcultured monthly and stored at 4°C after incubation for 2 days at 30°C. For purification of histidine-2-oxoglutarate aminotransferase, cells were grown in 100-litre batches on histidine-succinate medium as described by Hassall & Soutar (1974) and harvested in 'late-exponential phase. They were stored frozen at -1 8°C until required.…”

Section: Maintenance and Growth Of The Organismmentioning

confidence: 99%

“…The cells were thawed and resuspended in 5 vol. of 0.1M-potassium phosphate buffer, pH7.0, at 4°C and then passed three times through a Manton-Gaulin laboratory homogenizer (Hassall & Soutar, 1974) at a pressure of 55MPa (80001bf/in2). After disruption, cell debris was removed by centrifugation at 30000g for 40min.…”

Section: Ferasementioning

confidence: 99%

The purification and properties of l-histidine-2-oxoglutarate aminotransferase from Pseudomonas testosteroni

1975

Biochemical Journal

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Inducible L-histidine-2-oxoglutarate aminotransferase was purified some 170-fold from extracts of Pseudomonas testosteroni. 2. The preparation showed only one major component after electrophoresis on polyacrylamide gels, though additional minor bands were observed when samples concentrated on a DEAE-cellulose column were used. 3. The molecular weight of the enzyme was found to be approx. 70000 by chromatography on Sephadex G-200. 4. The purification scheme produced enzyme that was-inactive in the absence of pyridoxal 5'-phosphate. 5. The equilibrium constant for the reaction L-histidine+2-oxoglutarate = imidazolylpyruvate+L-glutamatewasO.49.6.Thereaction mechan'ism was Ping Pong. 7. The enzyme was shown to have only low activity towards aromatic amino acids and was highly specific for 2-oxoglutarate.

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“…L-Histidine ammonia-lyase, which converts L-histidine to urocanic acid and ammonia, is widely distributed in bacteria such as Pseudomonas fluorescens [l-51, P. aeruginosa [6], P.putida [7,8], P. testosteroni [9], Aerobacter aerogenes [lo, 111, Bacillus subtilis [12,13], B. cereus [14], Mycobacterium avium [15], Salmonella typhimurium [16], and Vibrio cholerae [17]. The enzyme occurs also in liver [18,19], blood serum [20], and stratum corneum [21] of higher animals and in plants such as spinach and sunflowers [22].…”

mentioning

confidence: 99%

“…The enzyme occurs also in liver [18,19], blood serum [20], and stratum corneum [21] of higher animals and in plants such as spinach and sunflowers [22]. However, there have been only three reports on the exhaustive purification of the enzyme [5,9,19]. Moreover, there has been no report on the crystallization of this enzyme.…”

mentioning

confidence: 99%

Crystalline l‐Histidine Ammonia‐Lyase of Achromobacter liquidum

Shibatani

Kakimoto

Chibata

1975

European Journal of Biochemistry

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Crystalline L-histidine ammonia-lyase of Achromobacter liquidum was prepared with a 24% recovery of the activity. The specific activity of the pure enzyme (63 mumol of urocanic acid min-1 mg-1) is similar to those so far reported for the enzyme from other sources. The purified enzyme appeared to be homogeneous by analytical disc electrophoresis and isoelectric focusing (pI = 4.95). The molecular weight determined by Sephadex G-200 gel filtration is 200000. The optimum pH is 8.2, and the optimum temperature is 50 degrees C. The enzyme showed strict specificity to L-histidine (Km = 3.6 mM). Several histidine derivatives are not susceptible to the enzyme but do inhibit the enzyme activity competitively; the most effective inhibitors are L-histidine methyl ester (Ki = 3.66 mM) and beta-imidazole lactic acid (Ki = 3.84 mM). L-Histidine hydrazide (Ki = 36 mM) and imidazole (Ki = 6 mM) noncompetitively inhibited the enzyme EDTA markedly inhibited enzyme activity and this inhibition were reversed by divalent metal ions such as Mn2+, Co2+ Zn2+, Ni2+, Mg2+, and Ca2+. These results suggest that the presence of divalent metal ions is necessary for the catalytic activity of histidine ammonia-lyase. Sodium borohydride and hydrogen peroxide inhibited the enzyme activity.

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Amino acid sequence of a peptide containing the active cysteine residue of histidine ammonia-lyase

Cited by 14 publications

References 25 publications

Sequence analysis of the hutH gene encoding histidine ammonia-lyase in Pseudomonas putida

Sequence analysis of the hutH gene encoding histidine ammonia-lyase in Pseudomonas putida

The purification and properties of l-histidine-2-oxoglutarate aminotransferase from Pseudomonas testosteroni

Crystalline l‐Histidine Ammonia‐Lyase of Achromobacter liquidum

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