• pepsin A EC 3.4.4.2: Now EC 3.4.23.2, pepsin B EC 3.4.4.3: Now EC 3.4.23.4, chymosin EC 3.4.4.4: Now EC 3.4.21.4, trypsin EC 3.4.4.5: Now EC 3.4.21.1, chymotrypsin...
    119 KB (15,553 words) - 03:35, 27 April 2024
  • Category:EC 1.1.3 (with oxygen as acceptor) Glucose oxidase EC 1.1.3.4 L-gulonolactone oxidase EC 1.1.3.8 Thiamine oxidase EC 1.1.3.23 Xanthine oxidase EC 1...
    33 KB (3,650 words) - 10:58, 5 May 2024
  • Thumbnail for Chymosin
    Chymosin (redirect from EC 3.4.23.4)
    Experimental Medicine and Biology. Vol. 306. pp. 23–37. doi:10.1007/978-1-4684-6012-4_3. ISBN 978-1-4684-6014-8. PMID 1812710. PDB: 4CMS​; Newman M, Safro M, Frazao...
    12 KB (1,306 words) - 17:48, 23 April 2024
  • Thumbnail for Caspase 3
    cell death protein Ced-3 and mammalian interleukin-1 beta-converting enzyme". The Journal of Biological Chemistry. 269 (49): 30761–4. doi:10.1016/S0021-9258(18)47344-9...
    29 KB (3,392 words) - 19:09, 24 June 2024
  • Thumbnail for Plasmin
    Plasmin (redirect from EC 3.4.21.7)
    Plasmin is an important enzyme (EC 3.4.21.7) present in blood that degrades many blood plasma proteins, including fibrin clots. The degradation of fibrin...
    15 KB (1,821 words) - 02:15, 10 March 2024
  • Thumbnail for Dipeptidyl peptidase-4
    pp. 27–32. doi:10.1007/0-387-32824-6_3. ISBN 978-0-387-29058-4. PMID 16700505. Barnett A (November 2006). "DPP-4 inhibitors and their potential role in...
    13 KB (1,620 words) - 21:56, 8 March 2024
  • Thumbnail for Trypsin
    Trypsin (redirect from EC 3.4.21.4)
    body temperatures. Cod trypsins include trypsin I with an activity range of 4 to 65 °C (39 to 149 °F) and maximal activity at 55 °C (131 °F), as well as...
    26 KB (2,827 words) - 03:33, 16 July 2024
  • tripeptide aminopeptidases have the code "EC 3.4.11.4", whose components indicate the following groups of enzymes: EC 3 enzymes are hydrolases (enzymes that...
    10 KB (895 words) - 11:45, 9 July 2024
  • Thumbnail for LexA repressor
    LexA repressor (redirect from EC 3.4.21.88)
    or LexA (Locus for X-ray sensitivity A) is a transcriptional repressor (EC 3.4.21.88) that represses SOS response genes coding primarily for error-prone...
    7 KB (722 words) - 04:30, 31 July 2024
  • compounds. EC 3.8.1.1 alkylhalidase EC 3.8.1.2 (S)-2-haloacid dehalogenase EC 3.8.1.3 haloacetate dehalogenase EC 3.8.1.4 moved to EC 1.97.1.10 EC 3.8.1.5...
    888 bytes (134 words) - 17:12, 8 May 2022
  • Thumbnail for Renin
    Renin (redirect from EC 3.4.23.15)
    modulated by the binding of HADHB, HuR and CP1 to a regulatory region in the 3' UTR. The gene for renin, REN, spans 12 kb of DNA and contains 8 introns....
    18 KB (2,105 words) - 03:55, 10 March 2024
  • Thumbnail for Papain
    Papain (redirect from EC 3.4.22.2)
    Papain, also known as papaya proteinase I, is a cysteine protease (EC 3.4.22.2) enzyme present in papaya (Carica papaya) and mountain papaya (Vasconcellea...
    18 KB (2,008 words) - 02:24, 14 August 2024
  • Andrew McDonald. EC 4.1.1.1: pyruvate decarboxylase EC 4.1.1.2: oxalate decarboxylase EC 4.1.1.3: Now recognized to be two enzymes EC 7.2.4.2 [oxaloacetate...
    62 KB (7,931 words) - 19:04, 4 January 2024
  • Thumbnail for Furin
    Furin (redirect from EC 3.4.21.75)
    wide variety of precursor proteins". The Biochemical Journal. 327 ( Pt 3) (3): 625–35. doi:10.1042/bj3270625. PMC 1218878. PMID 9599222. Bassi DE, Mahloogi...
    17 KB (2,288 words) - 15:22, 19 March 2024
  • Thumbnail for Botulinum toxin
    Botulinum toxin (redirect from EC 3.4.24.69)
    toxin in food. The estimated human median lethal dose of type A toxin is 1.3–2.1 ng/kg intravenously or intramuscularly, 10–13 ng/kg when inhaled, or 1000 ng/kg...
    116 KB (11,592 words) - 18:23, 17 August 2024
  • glycerophosphoinositol inositolphosphodiesterase (EC 3.1.4.43) is an enzyme that catalyzes the chemical reaction 1-(sn-glycero-3-phospho)-1D-myo-inositol + H2O ⇌ {\displaystyle...
    5 KB (505 words) - 14:21, 26 August 2023
  • Thumbnail for Cathepsin D
    Cathepsin D (redirect from EC 3.4.23.5)
    linked by the hydrophobic effect. The optimum pH for cathepsin D in vitro is 4.5-5.0. Cathepsin-D is an aspartic protease that depends critically on protonation...
    23 KB (2,619 words) - 05:01, 22 July 2024
  • Omptin (redirect from EC 3.4.21.87)
    Omptins (EC 3.4.23.49, protease VII, protease A, gene ompT proteins, ompT protease, protein a, Pla, OmpT) are a family of bacterial proteases. They are...
    11 KB (1,329 words) - 19:07, 28 July 2024
  • Thumbnail for Gamma-glutamyl hydrolase
    gamma-glutamyl hydrolase in a Japanese population". Biol. Pharm. Bull. 30 (4): 839–41. doi:10.1248/bpb.30.839. PMID 17409534. Gamma-glutamyl+hydrolase...
    8 KB (982 words) - 11:50, 3 June 2024
  • Thumbnail for MMP2
    MMP2 (redirect from EC 3.4.24.24)
    during cancer metastasis". Frontiers in Cell and Developmental Biology. 3: 4. doi:10.3389/fcell.2015.00004. PMC 4313772. PMID 25699257. Clark ES, Whigham...
    24 KB (2,812 words) - 11:56, 19 July 2024
  • Thumbnail for Factor X
    Factor X (redirect from EC 3.4.21.6)
    Coagulation factor X (EC 3.4.21.6), or Stuart factor, is an enzyme of the coagulation cascade, encoded in humans by F10 gene. It is a serine endopeptidase...
    27 KB (3,353 words) - 09:39, 12 August 2024
  • Thumbnail for Rhomboid protease
    S2CID 206334512.: 103  "Summary for family S54 (Rhomboid family)". MEROPS. "EC 3.4.21.105". Expasy. SIB Swiss Institute of Bioinformatics. Portal: Biology...
    42 KB (4,629 words) - 01:58, 16 December 2023
  • Progastricsin (redirect from EC 3.4.23.3)
    1988). "Primary structure of human pepsinogen C gene". J. Biol. Chem. 263 (3): 1382–5. doi:10.1016/S0021-9258(19)57314-8. PMID 3335549. Pals G, Azuma T...
    7 KB (920 words) - 07:29, 29 January 2023
  • Thumbnail for Factor XII
    Factor XII (redirect from EC 3.4.21.38)
    protein involved in coagulation. It is the zymogen form of factor XIIa (EC 3.4.21.38), an enzyme of the serine protease (or serine endopeptidase) class...
    27 KB (3,276 words) - 17:16, 10 May 2024
  • Thumbnail for Cathepsin B
    Cathepsin B (redirect from EC 3.4.22.1)
    International Journal of Cancer. 67 (4): 547–54. doi:10.1002/(SICI)1097-0215(19960807)67:4<547::AID-IJC14>3.0.CO;2-4. PMID 8759615. Pavlova A, Björk I (September...
    12 KB (1,346 words) - 00:48, 3 December 2023
  • gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. MMP-1 was the first vertebrate collagenase both purified to homogeneity as...
    13 KB (1,545 words) - 21:29, 14 December 2023
  • Thumbnail for Alanine aminopeptidase
    Membrane alanyl aminopeptidase (EC 3.4.11.2) also known as alanyl aminopeptidase (AAP) or aminopeptidase N (AP-N) is an enzyme that in humans is encoded...
    11 KB (1,330 words) - 08:31, 20 August 2024
  • Thumbnail for MMP3
    MMP3 (redirect from EC 3.4.24.17)
    Stromelysin-1 also known as matrix metalloproteinase-3 (MMP-3) is an enzyme that in humans is encoded by the MMP3 gene. The MMP3 gene is part of a cluster...
    26 KB (3,031 words) - 10:50, 15 January 2024
  • Thumbnail for Ficain
    Ficain (redirect from EC 3.4.22.3)
    Ficain also known as ficin, debricin, or higueroxyl delabarre (EC 3.4.22.3) is a proteolytic enzyme extracted from the latex sap from the stems, leaves...
    11 KB (1,346 words) - 21:42, 21 June 2024
  • Thumbnail for Metalloproteinase
    Metalloproteinase (category EC 3.4.24)
    metalloproteinases: Exopeptidases, metalloexopeptidases (EC number: 3.4.17). Endopeptidases, metalloendopeptidases (3.4.24). Well known metalloendopeptidases include...
    7 KB (759 words) - 02:51, 1 April 2024