Studies on Acylase Activity and Micro-organisms. XXV. Purification and Properties of Benzoylamino-acid Amidohydrolase in KT 801 (Pseudomonas sp.)

Kameda, Yukihiko; Kuramoto, Taijyu; Matsui, Kunihiko; Ebara, Takako

doi:10.1248/cpb.16.1023

Cited by 3 publications

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“…R6hr 17 ) reported the purification and properties of a hippurate hydrolase from Fusarium semitectum. Kameda et al 18 ) reo! ported on a N-benzoyl-amino acid amidohydrolase fr~m Pseudomonas sp.…”

Section: Discussionmentioning

confidence: 99%

Purification and Properties ofN-Benzoyl-l-alanine Amidohydrolase fromCorynebacterium equi

Miyagawa

Harada

Motoki

1986

Agricultural and Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

Purification and Properties ofN-Benzoyl-l-alanine Amidohydrolase fromCorynebacterium equi

Miyagawa

Harada

Motoki

1986

Agricultural and Biological Chemistry

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“…Micro-organisms capable of hydrolyzing hippurate are not uncommon and have been found among fungi such as Fusarium (Rohr, 1968) certain Streptomyces species (Ziegler & Kutzner, 1973) as well as within some species of Mycobacterium and Nomrdia (Gordon, 1966;Gordon 6 Horan, 1968). Among true bacteria, this property has been reported for species of Streptococcus (Gemmel & Hodgkiss, 1964), Pediococcus (Whittenbury, 1965), Corynebacterium (Brooks & Hucker, 1944), Beneckea (Baumann,Baumann & Mandel, 1971),Pseudomonw (Kameda, Kuramotot, Matsui & Ebara, 1968) and some Enterobacteriaceae (Thirst, 1957) ; it has not been studied previously in members of the genus BaciUus. The aim of the present study was to show whether such typical soil inhabitants as aerobic spore-forming bacilli were capable of hydrolyzing hippurate and whether this property could be used as a diagnostic aid within the genus.…”

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confidence: 92%

Detection of Hippurate Hydrolase among Bacillus Species by Thin Layer Chromatography and other Methods

Ottow

1974

Journal of Applied Bacteriology

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Summary. The ability of 111 isolates of 33 species of Bacillus to hydrolyze hippurate into benzoic acid and glycine was tested. All, other than the strains classified as B. badius, B. cereus var. mycoides, B. cereus var. thuringiensis, B. macquariensis, B. medusa, B. pacificus, B. psychrosaccharolyticus and some B. macerans and B. polymyxa strains, were positive by thin layer chromatography (TLC). Of the 4 methods compared (hippurate agar, the sulphuric acid method, precipitation with ferric chloride and TLC), only the TLC procedure allowed a rapid and definite detection of the hydrolytic product, benzoic acid. The use of hippurate hydrolase as an additional diagnostic aid in the differentiation of aerobic spore‐forming bacilli is discussed. Other characters were used to compare some recently described Bacillus spp. The combination B. cereus subsp. medusa n. subsp. is proposed.

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Enzymatic activity of Campylobacter jejuni hippurate hydrolase

Steele¹,

Marcone²,

Gyles³

et al. 2005

Protein Engineering, Design and Selection

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The hippurate hydrolase enzyme of Campylobacter jejuni was expressed in Escherichia coli as a six-histidine-tagged fusion protein. The purified recombinant enzyme was characterized to gain an understanding of the structure and activity of the hippurate hydrolase. The recombinant enzyme had a native molecular mass of 193+/- 11 kDa a reduced molecular mass of 42.4+/- 0.8 kDa, and possessed 1.98+/- 0.68 molecules of zinc per enzyme subunit molecule, suggesting that it was a homotetramer with two associated zinc ions. The enzyme was a metallocarboxypeptidase that was sensitive to silver, copper and ferrous ions, and displayed optimal activity at pH 7.5 and 50 degrees C. It hydrolyzed carboxypeptidase substrates in vitro, displaying its highest activity against N-benzoyl-linked small aliphatic amino acids. A high proportion of the enzyme structure consisted of highly ordered alpha-helix and beta-sheet sequences. An alignment of the amino acid sequence of the hippurate hydrolase enzyme with those of related enzymes with similar activities revealed several conserved amino acids, which might be involved in enzyme catalysis or metal ion binding for the enzyme. Site-directed mutagenesis of the recombinant enzyme demonstrated that the Asp(76), Aps(104), Glu(134), Glu(135), His(161) and His(356) positions were important for the catalytic activity of the enzyme.

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Studies on Acylase Activity and Micro-organisms. XXV. Purification and Properties of Benzoylamino-acid Amidohydrolase in KT 801 (Pseudomonas sp.)

Cited by 3 publications

References 0 publications

Purification and Properties ofN-Benzoyl-l-alanine Amidohydrolase fromCorynebacterium equi

Purification and Properties ofN-Benzoyl-l-alanine Amidohydrolase fromCorynebacterium equi

Detection of Hippurate Hydrolase among Bacillus Species by Thin Layer Chromatography and other Methods

Enzymatic activity of Campylobacter jejuni hippurate hydrolase

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