Halotolerant Collagenolytic Activity of Achromobacter iophagus

Welton, R. L.; Woods, David R.

doi:10.1099/00221287-75-1-191

Cited by 37 publications

(17 citation statements)

References 9 publications

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“…Strain 1.029 (Collection Institut Pasteur, Paris, France) is a subculture of the microorganism originally described as "A. iophagus" by Welton and Woods (34). Strain CIP 82.01 (Collection Institut Pasteur, Paris) of V. alginolyticus was isolated from a coastal seabed sediment in Madagascar and was identified by Richard and Lhuillier (28).…”

Section: Methodsmentioning

confidence: 99%

“…In 1973, Welton and Woods isolated and described the gram-negative aerobic bacterium Achromobacter iophagus (34). In the presence of collagen or macromolecular fragments of collagen (15), a subculture of this organism (strain 1.029) produces a collagenase having a very high specific activity (12,20).…”

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confidence: 99%

“…We undertook a comparative study to determine the differences between strain 1.029 isolated from a random selection of cured hides in South Africa (34) and a wild-type strain (strain CIP 82.01) of V . alginolyticus from a different geographical location (Madagascar) (28).…”

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Assignment of "Achromobacter iophagus" Strain I.029 to Vibrio alginolyticus Chemovar iophagus

Emod

Soubigou

Tong

et al. 1983

International Journal of Systematic Bacteriology

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RICHARD^Strain CIP 82.01 of Vibrio alginolyticus and strain 1.029 (previously designated "Achromobacter iophagus") were compared. Strain 1.029 produces a collagenase of high specific activity (Achrornobacter collagenase; EC 3.4.24.8). Collagenase production is induced in strain CIP 82.01 by collagen or macromolecular fragments of collagen in a manner similar to collagenase induction in strain 1.029; caseinolytic proteinase is constitutive. In this study we demonstrate that both strains also produce a constitutive extracellular endonuclease. Collagenases from both strains cleave either native collagen in its helical region or a similar synthetic peptide; both enzymes are inhibited by ethylenediamine tetraacetate, but not by diisopropyl fluorophosphate. The collagenase subunit (molecular weight, 35,000) of strain CIP 82.01 is similar in amino acid composition to the subunit of the strain 1.029 enzyme, although some of the aspartic and threonine residues in strain CIP 82.01 are replaced by glutamic and serine residues in strain 1.029. Surface radioiodination followed by two-dimensional electrophoresis showed that there are quantitative differences in the major outer membrane proteins of the two strains. Strains CIP 82.01 and 1.029 differ qualitatively in resistance to ampicillin and carbenicillin, in cellobiose fermentation, in ornithine decarboxylase activity, and in halophilism. We propose that strain 1.029, which was originally designated A . iophagus, be included within the species V. alginolyticus, but that this organism be distinguished from other strains of this species by the designation Vibrio alginolyticus chemovar iophagus, with the corresponding collagenase designated "iophagus collagenase" (EC 3.4.24.8).In 1973, Welton and Woods isolated and described the gram-negative aerobic bacterium Achromobacter iophagus (34). In the presence of collagen or macromolecular fragments of collagen (15), a subculture of this organism (strain 1.029) produces a collagenase having a very high specific activity (12,20). The structural and functional properties of this Achromobacter collagenase (EC 3.4.24.8), as well as the metabolism of strain 1.029, have been described in a series of papers by Woods et al. (21,26,27,29,35) and by workers in our laboratory (4,10,11,13,14,19,30).In a recent study (27), which confirmed the original observation of collagenase induction by macromolecular collagen fragments (15), Achromobacter iophagus was reclassified as a strain of Vibrio alginolyticus; however, a direct experimental comparison of strain 1.029 with a welldefined wild-type strain of V . alginolyticus has been lacking. It is well established that the other strains of the Vibrionaceae (23, 31) can be induced (by collagen and fragments of collagen) to produce collagenolytic and gelatinolytic enzymes.We undertook a comparative study to determine the differences between strain 1.029 isolated from a random selection of cured hides in South Africa (34) and a wild-type strain (strain CIP 82.01) of V . alginolyticus from a different ge...

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Section: Methodsmentioning

confidence: 99%

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confidence: 99%

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Assignment of "Achromobacter iophagus" Strain I.029 to Vibrio alginolyticus Chemovar iophagus

Emod

Soubigou

Tong

et al. 1983

International Journal of Systematic Bacteriology

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“…The collagenolytic strain previously isolated and classified as Achromobacter iophagus by Welton & Woods (1973) but recently reclassified as a V. alginolyticus strain was used (Reid et al, 1980). The bacterium was maintained on the complex medium of Welton & Woods (1973). The peptone medium, G .…”

Section: Methodsmentioning

confidence: 99%

“…Vibrio alginolyticus is an aerobic, halotolerant, Gram-negative bacterium which produces an extracellular collagenase and extracellular alkaline protease enzymes during the stationary growth phase (Welton & Woods, 1973,1975Reid etal., 1978Reid etal., ,1980Longet al, 1981). Common features in the control of collagenase and alkaline protease enzymes by V. alginolyticus include end-product and catabolite repression (Reid et al, 1978;Long et al, 1981) and specific regulation by temperature and oxygen (Hare et al, 198 1).…”

Section: Introductionmentioning

confidence: 99%

Regulation of Hut Enzymes and Extracellular Protease Activities in Vibrio alginolyticus hut Mutants

et al. 1982

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The production of alkaline protease, collagenase and histidine utilization (Hut) enzymes by Vibrio alginolyticus wild-type, hutHl and hut UI strains was investigated. Alkaline protease synthesis was stimulated by histidine and urocanic acid in the wild-type and hutUl strains. In the hutHl mutant alkaline protease production was stimulated by urocanic acid and not by histidine. The Hut enzymes in the wild-type strain were coordinately induced by histidine. Urocanase and formimino-hydrolase were induced by histidine in the hutHl mutant which lacked histidase and was not able to convert histidine to urocanic acid. Collagenase production in peptone medium was inhibited in the hut mutants. It is concluded that in V. alginolyticus urocanic acid regulates alkaline protease synthesis but that the Hut enzymes are induced by histidine. The involvement of the Hut genetic system in the regulation of alkaline protease and collagenase synthesis is discussed.

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Some newly characterized collagenases from procaryotes and lower eucaryotes

Keil¹

1979

Mol Cell Biochem

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Chemical and enzymatic properties of four collagenases newly isolated from anaerobic Clostridium histolyticum, aerobic Achromobacter iophagus, and from two lower eucaryotes, the fungus Entomophthora coronata and the insect Hypoderma lineatum are reviewed. The problems of their biosynthesis and precursors, namely the effect of induction of collagenase and neutral proteinase in Achromobacter by their macromolecular substrates are discussed. The two bacterial collagenases are Zn-metallo-enzymes; the highly purified Clostridium collagenase contains cyst(e)ine, serine phosphate and tryptophan additionally to amino acids reported previously. Achromobacter collagenase has the highest specific activity of all collagenases; it yields by autolysis enzymatically active degraded forms. The active dimer is composed of two identical subunits of molecular weight 35,000. Similarities between Achromobacter collagenase, thermolysin and Bacillus subtilis neutral proteinase in molecular weight, amino acid composition, and amino acids important for the active sites are discussed. The two collagenases from low eucaryotes are serine proteinases; Hypoderma collagenase is homologous to the trypsin family in the amino terminal sequence. The initial cleavage of native collagen by highly purified bacterial collagenases occurs in the central helical part of the alpha chains and not progressively from the amino terminal end. One of the two initial cleavages produced by Achromobacter collagenase is situated in the region cleaved specifically by vertebrate collagenases, but with different bond specificity. The same is true for the insect collagenase. Entomophthora collagenase is a proteinase of broad specificity which also cleaves collagen in its helical parts. All four collagenases also degrade other proteins according to their bond specificity.

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Halotolerant Collagenolytic Activity of Achromobacter iophagus

Cited by 37 publications

References 9 publications

Assignment of "Achromobacter iophagus" Strain I.029 to Vibrio alginolyticus Chemovar iophagus

Assignment of "Achromobacter iophagus" Strain I.029 to Vibrio alginolyticus Chemovar iophagus

Regulation of Hut Enzymes and Extracellular Protease Activities in Vibrio alginolyticus hut Mutants

Some newly characterized collagenases from procaryotes and lower eucaryotes

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