Penicillin acylases revisited: importance beyond their industrial utility

被引:17
作者
Avinash, Vellore Sunder [1 ]
Pundle, Archana Vishnu [1 ]
Ramasamy, Sureshkumar [1 ]
Suresh, Cheravakkattu Gopalan [1 ]
机构
[1] CSIR, Natl Chem Lab, Div Biochem Sci, Pune 411008, Maharashtra, India
关键词
beta-lactam; choloyl glycine; in vivo role; Ntn hydrolases; pathogenicity; quorum sensing; regulation; signalling; BILE-SALT HYDROLASE; HOMOSERINE LACTONE ACYLASE; N-TERMINAL NUCLEOPHILE; QUORUM-SENSING SIGNALS; ACULEACIN-A-ACYLASE; V-ACYLASE; ESCHERICHIA-COLI; SUBSTRATE-SPECIFICITY; MOLECULAR-CLONING; 6-AMINOPENICILLANIC ACID;
D O I
10.3109/07388551.2014.960359
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
It is of great importance to study the physiological roles of enzymes in nature; however, in some cases, it is not easily apparent. Penicillin acylases are pharmaceutically important enzymes that cleave the acyl side chains of penicillins, thus paving the way for production of newer semi-synthetic antibiotics. They are classified according to the type of penicillin (G or V) that they preferentially hydrolyze. Penicillin acylases are also used in the resolution of racemic mixtures and peptide synthesis. However, it is rather unfortunate that the focus on the use of penicillin acylases for industrial applications has stolen the spotlight from the study of the importance of these enzymes in natural metabolism. The penicillin acylases, so far characterized from different organisms, show differences in their structural nature and substrate spectrum. These enzymes are also closely related to the bacterial signalling phenomenon, quorum sensing, as detailed in this review. This review details studies on biochemical and structural characteristics of recently discovered penicillin acylases. We also attempt to organize the available insights into the possible in vivo role of penicillin acylases and related enzymes and emphasize the need to refocus research efforts in this direction.
引用
收藏
页码:303 / 316
页数:14
相关论文
共 125 条
  • [1] BEIJERINCKIA-INDICA VAR PENICILLANICUM PENICILLIN-V ACYLASE - ENHANCED ENZYME-PRODUCTION BY CATABOLITE REPRESSION-RESISTANT MUTANT AND EFFECT OF SOLVENTS ON ENZYME-ACTIVITY
    AMBEDKAR, SS
    DESHPANDE, BS
    SUDHAKARAN, VK
    SHEWALE, JG
    [J]. JOURNAL OF INDUSTRIAL MICROBIOLOGY, 1991, 7 (03): : 209 - 214
  • [2] Biotechnological applications of penicillin acylases:: state-of-the-art
    Arroyo, M
    de la Mata, I
    Acebal, C
    Castillón, MP
    [J]. APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 2003, 60 (05) : 507 - 514
  • [3] Structural modelling of substrate binding and inhibition in penicillin V acylase from Pectobacterium atrosepticum
    Avinash, V. S.
    Panigrahi, Priyabrata
    Suresh, C. G.
    Pundle, Archana V.
    Ramasamy, Sureshkumar
    [J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2013, 437 (04) : 538 - 543
  • [4] Tobramycin at subinhibitory concentration inhibits the RhlI/R quorum sensing system in a Pseudomonas aeruginosa environmental isolate
    Babic, Fedora
    Venturi, Vittorio
    Maravic-Vlahovicek, Gordana
    [J]. BMC INFECTIOUS DISEASES, 2010, 10
  • [5] COMPARISON OF LACTOBACILLUS STRAINS WITH RESPECT TO BILE-SALT HYDROLASE ACTIVITY, COLONIZATION OF THE GASTROINTESTINAL-TRACT, AND GROWTH-RATE OF THE MURINE HOST
    BATEUP, JM
    MCCONNELL, MA
    JENKINSON, HF
    TANNOCK, GW
    [J]. APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1995, 61 (03) : 1147 - 1149
  • [6] Bile salt hydrolase activity in probiotics
    Begley, M
    Hill, C
    Gahan, CGM
    [J]. APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2006, 72 (03) : 1729 - 1738
  • [7] Contribution of three bile-associated loci, bsh, pva, and btlB, to gastrointestinal persistence and bile tolerance of Listeria monocytogenes
    Begley, M
    Sleator, RD
    Gahan, CGM
    Hill, C
    [J]. INFECTION AND IMMUNITY, 2005, 73 (02) : 894 - 904
  • [8] The quorum-quenching N-acyl homoserine lactone acylase PvdQ is an Ntn-hydrolase with an unusual substrate-binding pocket
    Bokhove, Marcel
    Jimenez, Pol Nadal
    Quax, Wim J.
    Dijkstra, Bauke W.
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2010, 107 (02) : 686 - 691
  • [9] A PROTEIN CATALYTIC FRAMEWORK WITH AN N-TERMINAL NUCLEOPHILE IS CAPABLE OF SELF-ACTIVATION
    BRANNIGAN, JA
    DODSON, G
    DUGGLEBY, HJ
    MOODY, PCE
    SMITH, JL
    TOMCHICK, DR
    MURZIN, AG
    [J]. NATURE, 1995, 378 (6555) : 416 - 419
  • [10] Cloning, overexpression, and characterization of a novel thermostable penicillin g acylase from Achromobacter xylosoxidans:: Probing the molecular basis for its high thermostability
    Cai, G
    Zhu, SC
    Yang, S
    Zhao, GP
    Jiang, WH
    [J]. APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2004, 70 (05) : 2764 - 2770