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enzyme (lysozyme)

 
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  EC 1: Oxidoreductases
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  EC 4: Lyases
    EC 4.1
      EC 4.1.1
      EC 4.1.2
      EC 4.1.3
        EC 4.1.3.1
        EC 4.1.3.2
        EC 4.1.3.3
        EC 4.1.3.4
        EC 4.1.3.5
        EC 4.1.3.6
        EC 4.1.3.7
        EC 4.1.3.8
        EC 4.1.3.9
        EC 4.1.3.10
        EC 4.1.3.11
        EC 4.1.3.12
        EC 4.1.3.13
        EC 4.1.3.14
        EC 4.1.3.15
        EC 4.1.3.16
        EC 4.1.3.17
        EC 4.1.3.18
        EC 4.1.3.19
        EC 4.1.3.20
        EC 4.1.3.21
        EC 4.1.3.22
        EC 4.1.3.23
        EC 4.1.3.24
        EC 4.1.3.25
        EC 4.1.3.26
        EC 4.1.3.27
        EC 4.1.3.28
        EC 4.1.3.29
        EC 4.1.3.30
        EC 4.1.3.31
        EC 4.1.3.32
        EC 4.1.3.33
        EC 4.1.3.34
        EC 4.1.3.35
        EC 4.1.3.36
        EC 4.1.3.37
        EC 4.1.3.38
        EC 4.1.3.39
        EC 4.1.3.40
      EC 4.1.99
    EC 4.2
    EC 4.3
    EC 4.4
    EC 4.5
    EC 4.6
    EC 4.99
  EC 5: Isomerases
  EC 6: Ligases
  General information:
  Catalytic mechanism
  Enzyme kinetics
  Inhibitors
  Enzymes in industry

EC 4.1.3.39 - 4- hydroxy- 2- oxopentanoate pyruvate- lyase (acetaldehyde- forming) (4- hydroxy- 2- oxovalerate aldolase)



3D structures of EC 4.1.3.39 - 4-hydroxy-2-oxovalerate aldolase in Protein Data Bank

updated: 6 January 2022, 2:15

In total: 3 PDB structures of EC 4.1.3.39 - 4-hydroxy-2-oxovalerate aldolase:
  1. 4jn6: Crystal Structure of The Aldolase-dehydrogenase Complex from Mycobacterium Tuberculosis Hrv37
  2. 4lrs: Crystal and Solution Structures of The Bifunctional Enzyme (aldolase/aldehyde Dehydrogenase) from Thermomonospora Curvata, Reveal a Cofactor-binding Domain Motion during Nad+ and Coa Accommodation Whithin The Shared Cofactor-binding Site
  3. 4lrt: Crystal and Solution Structures of The Bifunctional Enzyme (aldolase/aldehyde Dehydrogenase) from Thermomonospora Curvata, Reveal a Cofactor-binding Domain Motion during Nad+ and Coa Accommodation Whithin The Shared Cofactor-binding Site
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