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Overview for MACiE Entry M0218

Version history

General Information

EC Number: 3.1.1.3 (A member of the Hydrolases, Acting on ester bonds, Carboxylic-ester hydrolases)

Enzyme Name: triacylglycerol lipase

Biological Species: Equus caballus (Horse)

Catalytic Chain UniprotKB Accession Codes:

  • P29183 - Pancreatic triacylglycerol lipase

Representative PDB Code: 1hpl - HORSE PANCREATIC LIPASE. THE CRYSTAL STRUCTURE AT 2.3ANGSTROMS RESOLUTION (Resolution = 2.30 Å).

Catalytic CATH Codes:

"Other" CATH Codes:

Display structure information

Overall Reaction:

Image of Triacylglycerol

Image of Water

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Image of Carboxylate

Image of Diacylglycerol

Triacylglycerol
C00422
CHEBI:17855
Water
C00001
CHEBI:15377
Carboxylate
C00060
CHEBI:18245
Diacylglycerol
C00165
CHEBI:17815

Overall Comment: Although this enzyme binds a calcium ion, it is distant from the active site and not involved in catalysis.


View similar reactions


Stepwise Description of the Reaction

Step 1His263 (part of a Ser-His-Asp triad) deprotonates Ser152, which attacks the carboxy carbon of the triacylglycerol substrate in a nucleophilic addition.
Step 2The oxyanion collapses, initiating an elimination of the diacylglycerol product, which deprotonates His263 and acylated Ser152.
Step 3His263 deprotonates water, which attacks the carboxyl carbon of the acylated Ser152 in a nucleophilic addition.
Step 4The oxyanion collapses, initiating an elimination of the carboxylate product, and Ser152, which deprotonates His263.

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
Ser 152 A Side Chain
His 263 A Side Chain
Asp 176 A Side Chain
Phe 77 A Main Chain Amide
Leu 153 A Main Chain Amide

References

  1. M. E. Lowe (1997), J. Nutr., 127, 549-557. Molecular mechanisms of rat and human pancreatic triglyceride lipases.
    Medline: 9109604
  2. Y. Bourne et al. (1994), J. Mol. Biol., 238, 709-732. Horse pancreatic lipase. The crystal structure refined at 2.3 A resolution.
    Medline: 8182745
  3. R.J. Kazlauskas (1994), Trends Biotechnol., 12, 464-472. Elucidating structure-mechanism relationships in lipases: prospects for predicting and engineering catalytic properties.
    Medline: 7765546
  4. H. van Tilbeurgh et al. (1993), Nature, 362, 814-820. Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography.
    Medline: 8479519

Homologue information for M0218 (1hpl)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)



Entries with at least one Catalytic CATH code in common (different mechanisms):

MACiE Entry Enzyme Name
EC Number
PDB code CATH code Composite
Reaction Similarity
Catalytic Machinery
Similarity
M0248 chloride peroxidase
1.11.1.10
1a7u 3.40.50.1820
0.83780.6381Compare
M0169 dipeptidyl-peptidase IV
3.4.14.5
1pfq 3.40.50.1820
0.75750.3208Compare
M0005 carboxypeptidase D
3.4.16.6
1whs 3.40.50.1820
0.75750.3856Compare
M0217 hydroxynitrilase
4.1.2.37
1sc9 3.40.50.1820
0.29030.4074Compare

View a comparison of the other reactions in MACiE with the CATH domain 3.40.50.1820


Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
Link to MetaCyc Link to KEGG Link to BRENDA Link to ExplorENZ
Link to EzCatDB

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catalytic activity (molecular function)
triglyceride lipase activity (molecular function)
extracellular region (cellular component)
lipid metabolic process (biological process)
steroid metabolic process (biological process)
lipid catabolic process (biological process)
hydrolase activity (molecular function)
intestinal cholesterol absorption (biological process)
retinyl-palmitate esterase activity (molecular function)
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