Реферат: Penicillin acylase from Alcaligenes faecalis has a very high affinity for both natural (benzylpenicillin, K m=0.0042 mM) and colorimetric (6-nitro-3-phenylacetamidobenzoic acid, K m=0.0045 mM) substrates as well as the product of their hydrolysis, phenylacetic acid (K i=0.016 mM). The enzyme is partially inhibited at high benzylpenicillin concentrations but the triple SES complex formed still retains 43% of the maximal catalytic activity; the affinity of benzylpenicillin for the second substrate molecule binding site is much lower (K S′=54 mM) than for the first one. Phenylmethylsulfonyl fluoride was shown to be a very effective irreversible inhibitor, completely inactivating the penicillin acylase from A. faecalis in a few minutes at micromolar concentrations; this compound was used for enzyme active site titration. The absolute values of the determined kinetic parameters for enzymatic hydrolysis of 6-nitro-3-phenylacetamidobenzoic acid (k cat=95 s−1 and k cat/K m=2.1×10−7 M−1 s−1) and benzylpenicillin (k cat=54 s−1 and k cat/K m=1.3×10−7 M−1 s−1) by penicillin acylase from A. faecalis were shown to be highest of all the enzymes of this family that have so far been studied.

Библиографическая ссылка: Svedas V. , Guranda D. , van Langen L. , van Rantwijk F. , Sheldon R.
Kinetic study of penicillin acylase from Alcaligenes faecalis
FEBS Letters. 1997. V.417. N3. P.414-418. DOI: 10.1016/s0014-5793(97)01289-1 Scopus OpenAlex CAPlusCA PMID

Идентификаторы БД:

≡ Scopus:	2-s2.0-0030853283 Добавил Робот 6 нояб. 2025 г.
≡ OpenAlex:	W1969902013 Добавил Робот 6 нояб. 2025 г.
≡ Chemical Abstracts:	1997:723791 Добавил Зибарева И.В. 3 нояб. 2025 г.
≡ Chemical Abstracts (print):	128:31768 Добавил Зибарева И.В. 3 нояб. 2025 г.
≡ PMID (PubMed):	9409763 Добавил Зибарева И.В. 3 нояб. 2025 г.

Цитирование в БД:

≡ Scopus	63
≡ OpenAlex	61

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