EC number:3.5.2.6

Enzyme

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EC Tree
     3. Hydrolases
        3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
            3.5.2 In cyclic amides
ID:3.5.2.6
Description:Beta-lactamase.
Alternative Name: Penicillinase.
Cephalosporinase.
Prosite: PDOC00606; PDOC00134;
PDB:
PDBScop
5HH4 8061852; 8061853; 8061852; 8061853; 8061852; 8061853; 8061852; 8061853;
5EWA 8061852; 8061853; 8061852; 8061853; 8061852; 8061853; 8061852; 8061853;
5EV8 8061852; 8061853; 8061852; 8061853; 8061852; 8061853; 8061852; 8061853;
5EV6 8061852; 8061853; 8061852; 8061853; 8061852; 8061853; 8061852; 8061853;
1WUP 8061852; 8061853; 8061852; 8061853; 8061852; 8061853; 8061852; 8061853;
 » show all
Cath: 3.40.710.10; 3.60.15.10; 1.25.40.10; 3.40.190.10; 2.60.410.10;

3D structure

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PDB

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5HH4; 5EWA; 5EV8; 5EV6; 1WUP; 4C1G; 4C1F; 2DOO; 1VGN; 1DD6; 5Y5B; 4DXC; 3T9M; 3SW3; 3IOG; 3IOF; 3F9O; 2QDS; 2GKL; 1X8I; 1X8H; 1X8G; 4KG6; 4KG5; 6DPZ; 6DPY; 6DPX; 6DPT; 4OLG; 4OLD; 4OKP; 4LV3; 4LV2; 4LV1; 4LV0; 4KZB; 4KZA; 4KZ9; 4KZ8; 4KZ7; 4KZ6; 4KZ4; 4KZ3; 4KG2; 4JXW; 4JXV; 4JXS; 4JXG; 4E3O; 4E3N; 4E3M; 4E3L; 4E3K; 4E3J; 4E3I; 3O88; 3O87; 3O86; 3IXH; 3IXG; 3IXD; 3IXB; 3IWQ; 3IWO; 3IWI; 3GVB; 3GV9; 3GTC; 3GSG; 3GRJ; 3GR2; 3GQZ; 3BM6; 3BLS; 2RCX; 2R9X; 2R9W; 2PU4; 2PU2; 2P9V; 2I72; 2HDU; 2HDS; 2HDR; 2HDQ; 2FFY; 2BLS; 1XGJ; 1XGI; 1PI5; 1PI4; 1O07; 1MY8; 1MXO; 1LLB; 1LL9; 1LL5; 1L2S; 1L0F; 1KVM; 1KE4; 1KE3; 1KE0; 1KDW; 1KDS; 1IEM; 1IEL; 1I5Q; 1GA9; 1FSY; 1FSW; 1FCO; 1FCN; 1FCM; 1C3B; 4KEN; 3C7V; 1JTG; 3C4P; 3C4O; 2G2U; 1S0W; 3C7U; 2B5R; 4RX2; 3JYI; 4IBX; 6B2N; 6AYK; 6APA; 5KPU; 5KKF; 5IQ8; 5I63; 5I52; 5HW5; 5HW1; 5HVI; 4MEZ; 3TOI; 5NPO; 4ZJ1; 4RVA; 4IBR; 4GKU; 3DTM; 3CMZ; 2V20; 2V1Z; 1ZG4; 1YT4; 1XPB; 1TEM; 1PZP; 1PZO; 1NYY; 1NYM; 1NY0; 1NXY; 1M40; 1LI9; 1LI0; 1LHY; 1JWZ; 1JWV; 1JWP; 1JVJ; 1FQG; 1ESU; 1ERQ; 1ERO; 1ERM; 1CK3; 1BTL; 1BT5; 1AXB; 1RGY; 1HZO; 2CC1; 2G2W; 5EE8; 4ZAM; 4R3B; 4MBK; 4MBH; 4MBF; 4JPM; 4GDB; 4GD8; 4GD6; 4FH4; 4FCF; 3V5M; 3V50; 3OPR; 3OPP; 3OPL; 3OPH; 3MXS; 3MXR; 3MKF; 3MKE; 3D4F; 2ZD8; 2H5S; 2H10; 2H0Y; 2H0T; 2A49; 2A3U; 1VM1; 1TDL; 1TDG; 1SHV; 1RCJ; 1Q2P; 1ONG; 3KNS; 3KNR; 3FCZ; 2NZE; 2BGA; 2BG8; 2BG7; 2BG6; 2BG2; 2BFZ; 2BFL; 2BFK; 2BC2; 1BC2; 6F2N; 6EWE; 6EUM; 5W8W; 5JMX; 5FQB; 5FQA; 4TYT; 4NQ6; 4NQ5; 4NQ4; 4C1H; 4C1C; 4C09; 3I15; 3I14; 3I13; 3I11; 3I0V; 3BC2; 2NZF; 2NYP; 2NXA; 2M5D; 2M5C; 1MQO; 1DXK; 1BVT; 1BMC; 4WZ5; 2HP5; 1K57; 1K56; 1K55; 1K54; 1EWZ; 1E3U; 5MOZ; 5MOX; 5MNU; 4S2O; 2WGW; 2WGV; 2WGI; 2RL3; 2HPB; 2HP9; 2HP6; 1K6R; 1FOF; 1JTD; 1E25; 1BSG; 5ZG6; 5ZFT; 5ZFL; 5LWF; 5GHZ; 5GHY; 5GHX; 4N9L; 4N9K; 4N92; 4N1H; 4BLM; 3SOI; 3SH9; 3SH8; 3SH7; 3M2K; 3M2J; 3B3X; 2WK0; 2BLM; 1W7F; 1MBL; 1I2W; 1I2S; 4M3K; 3LY4; 3LY3; 1PIO; 1OME; 3BLM; 1KGG; 1KGF; 1KGE; 1GHP; 1GHM; 1GHI; 1BLP; 1BLH; 1BLC; 1ALQ; 4R4S; 4R4R; 4QY6; 4QY5; 4ID4; 1G6A; 1G68; 5DPX; 2H6A; 2GFK; 2GFJ; 2FU9; 2FU8; 2FU7; 2FU6; 2FM6; 5HH6; 5HH5; 5EVK; 5EVD; 5EVB; 2QDT; 2HB9; 2AIO; 1SML; 4ZNB; 3ZNB; 2ZNB; 2BMI; 1KR3; 1HLK; 1A8T; 1A7T; 5KSC; 5KMW; 5G18; 4C3Q; 4BD1; 4BD0; 2ZQD; 2ZQC; 2ZQA; 2ZQ9; 2ZQ8; 2ZQ7; 2XR0; 2XQZ; 2WYX; 1WE4; 1IYS; 1IYQ; 1IYP; 1IYO; 1BZA; 1CI9; 1CI8; 1N9B; 1M2X; 6B6F; 6B6E; 6B6D; 6B6C; 6B6B; 6B6A; 6B69; 6B68; 6B5Y; 6B5X; 5XHR; 5OYO; 5NJ2; 5A93; 5A92; 5A91; 5A90; 4XUX; 4X6T; 4X69; 4X68; 4WZ4; 4WYY; 4QHC; 4Q8I; 4OOY; 4NK3; 4KZ5; 4JLF; 4HEF; 4GZB; 4EBP; 4EBN; 4EBL; 4DXB; 4DF6; 3ZHH; 3VFH; 3VFF; 3S4X; 3S22; 3S1Y; 3NDG; 3NDE; 3NCK; 3NC8; 3NBL; 3N8S; 3N8R; 3N8L; 3N7W; 3N6I; 3N4I; 3M6H; 3M6B; 3IQA; 3FAI; 3DWZ; 3CG5; 3BYD; 2WZZ; 2WZX; 2QZ6; 2Q9N; 2Q9M; 2GDN; 1ZNB; 1Y54; 1XXM; 1XX2; 1RGZ; 1GCE; 1BLS;

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.2.6
BRENDA Enzyme Link: BRENDA 3.5.2.6
KEGG Enzyme Link: KEGG3.5.2.6
BioCyc Enzyme Link: BioCyc 3.5.2.6
ExPASy Enzyme Link: ExPASy3.5.2.6
EC2PDB Enzyme Link: EC2PDB 3.5.2.6
ExplorEnz Enzyme Link: ExplorEnz 3.5.2.6
PRIAM enzyme-specific profiles Link: PRIAM 3.5.2.6
IntEnz Enzyme Link: IntEnz 3.5.2.6
MEDLINE Enzyme Link: MEDLINE 3.5.2.6

EC number:3.5.2.6

MSA:

3.5.2.6;
Phylogenetic Tree:

3.5.2.6;
Uniprot:
M-CSA:
RHEA:20401 a beta-lactam + H2O = a substituted beta-amino acid
RULE(radius=1) [*:1]-[N;H0;+0:2]1-[*:3]-[*:4]-[C;H0;+0:5]-1=[*:6].[OH2;+0:7]>>[*:1]-[NH;+0:2]-[*:3]-[*:4]-[C;H0;+0:5](=[*:6])-[OH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Purification, characterization, and kinetic studies of a soluble Bacteroides fragilis metallo-beta-lactamase that provides multiple antibiotic resistance.Wang Z, Benkovic SJ1998 Aug 289712862
Recombinant expression and characterization of the major beta-lactamase of Mycobacterium tuberculosis.Voladri RK, Lakey DL, Hennigan SH, Menzies BE, Edwards KM, Kernodle DS1998 Jun9624479
Characterization and sequence of the Chryseobacterium (Flavobacterium) meningosepticum carbapenemase: a new molecular class B beta-lactamase showing a broad substrate profile.Rossolini GM, Franceschini N, Riccio ML, Mercuri PS, Perilli M, Galleni M, Frere JM, Amicosante G1998 May 159576862
Molecular characterization of an enterobacterial metallo beta-lactamase found in a clinical isolate of Serratia marcescens that shows imipenem resistance.Osano E, Arakawa Y, Wacharotayankun R, Ohta M, Horii T, Ito H, Yoshimura F, Kato N1994 Jan8141584
The production and molecular properties of the zinc beta-lactamase of Pseudomonas maltophilia IID 1275.Bicknell R, Emanuel EL, Gagnon J, Waley SG1985 Aug 13931629
Purification and characterization of inducible beta-lactamases in Aeromonas spp.Iaconis JP, Sanders CC1990 Jan2327760
Biochemical and structural characterization of Mycobacterium tuberculosis beta-lactamase with the carbapenems ertapenem and doripenem.Tremblay LW, Fan F, Blanchard JS2010 May 420353175
Characterization of a new metallo-beta-lactamase gene, bla(NDM-1), and a novel erythromycin esterase gene carried on a unique genetic structure in Klebsiella pneumoniae sequence type 14 from India.Yong D, Toleman MA, Giske CG, Cho HS, Sundman K, Lee K, Walsh TR2009 Dec19770275
The structure of the dizinc subclass B2 metallo-beta-lactamase CphA reveals that the second inhibitory zinc ion binds in the histidine site.Bebrone C, Delbrück H, Kupper MB, Schlömer P, Willmann C, Frère JM, Fischer R, Galleni M, Hoffmann KM2009 Oct19651913
Meropenem-clavulanate is effective against extensively drug-resistant Mycobacterium tuberculosis.Hugonnet JE, Tremblay LW, Boshoff HI, Barry CE 3rd, Blanchard JS2009 Feb 2719251630
Irreversible inhibition of the Mycobacterium tuberculosis beta-lactamase by clavulanate.Hugonnet JE, Blanchard JS2007 Oct 3017915954
Competitive inhibitors of the CphA metallo-beta-lactamase from Aeromonas hydrophila.Horsfall LE, Garau G, Liénard BM, Dideberg O, Schofield CJ, Frère JM, Galleni M2007 Jun17307979
Crystal structure and activity studies of the Mycobacterium tuberculosis beta-lactamase reveal its critical role in resistance to beta-lactam antibiotics.Wang F, Cassidy C, Sacchettini JC2006 Aug16870770
A metallo-beta-lactamase enzyme in action: crystal structures of the monozinc carbapenemase CphA and its complex with biapenem.Garau G, Bebrone C, Anne C, Galleni M, Frère JM, Dideberg O2005 Jan 2815588826