1967
DOI: 10.1099/00221287-46-1-111
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The Aliphatic Acylamide Amidohydrolase of Mycobacterium smegmatis: Its Inducible Nature and Relation to Acyl-Transfer to Hydroxylamine

Abstract: SUMMARYMycobacterium srnegrnatis NCTC 8 159 grew well in a minimal medium with succinate or acetamide as sole carbon source. Washed bacteria or cell-free extracts hydrolyzed 15 monocarboxylic amides, but not 4 related N-substituted amides. Formamide was the best substrate, followed by n-butyramide. Extracts of bacteria grown on acetamide hydrolyzed formamide about 60 times and butyramide about 20 times as rapidly as bacteria grown on succinate. Other short-chain fatty acylamides were also more rapidly hydrolyz… Show more

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Cited by 54 publications
(50 citation statements)
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“…The two least related proteins with proven biochemical function are the formamidase from Methylophilus methylotrophus (56) and the well-characterized acetamidase from Mycobacterium smegmatis (37). These two enzymes, which both showed 25% overall sequence identity to LamA, enable the bacteria to grow on formamide as a source of nitrogen (18,57).…”
Section: Resultsmentioning
confidence: 99%
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“…The two least related proteins with proven biochemical function are the formamidase from Methylophilus methylotrophus (56) and the well-characterized acetamidase from Mycobacterium smegmatis (37). These two enzymes, which both showed 25% overall sequence identity to LamA, enable the bacteria to grow on formamide as a source of nitrogen (18,57).…”
Section: Resultsmentioning
confidence: 99%
“…The enzymes from M. methylotrophus and M. smegmatis have been (partially) purified and biochemically characterized and appear to be closely related, as reflected by their 57% sequence identity and the cross-reactivity of antisera prepared against the two enzymes (56). They exhibit an extremely narrow substrate specificity, with the highest activity toward formamide and much lower activities toward short-chain aliphatic amides such as propionamide, butyramide, and acetamide (18,57), exactly the substrates that the O. anthropi L-amidase cannot convert. Activities toward other types of substrates as well as investigations of potential enantioselectivity have not been reported.…”
Section: Discussionmentioning
confidence: 99%
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“…When we provided PAM as an N-source, both PAM-specific activity and amidase activity specific for low MW amides was exhibited, in both enrichment cultures and soils. Amidases that demonstrate broad substrate specificities have been reported (Draper, 1967;Maestracci et al, 1984), although the enzyme preparations used were either crude or only partially purified, consequently could represent a suite of amidase enzymes. There is also a report of multiple amidase isozymes, each with a limited substrate specificity, produced simultaneously by Aspergillus nidulans when induced by a single small amide (Hynes and Pateman, 1970).…”
Section: Discussionmentioning
confidence: 99%
“…This is the first report of an amidase, in culture or in soil, capable of attacking a polymer in this size range (1-2 x 107 MW). Amidase activity has been identified in numerous genera of bacteria, including Rhodococcus (Nawaz et al, 1994), Bacillus (Thalenfeld and Grosswicz, 1976), Mycobacterium (Draper, 1967), Brevibacterium (Maestracci et al, 1984), Alcaligenes (Friedrich and Mitrenga, 1981), and Pseudomonas (Kelly and Clarke, 1962;Clarke, 1970;Ciskanik et al, 1995). In addition, amidase activity has been demonstrated in several fungi, including Aspergillus (Hynes and Pateman, 1970) and Fusarium (Reichel et al, 1991).…”
Section: Discussionmentioning
confidence: 99%