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Overview for MACiE Entry M0217

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General Information

EC Number: 4.1.2.37 (A member of the Lyases, Carbon-carbon lyases, Aldehyde-lyases)

Enzyme Name: hydroxynitrilase

Biological Species: Hevea brasiliensis (Para rubber tree)

Catalytic Chain UniprotKB Accession Codes:

  • P52704 - (S)-hydroxynitrile lyase

Representative PDB Code: 1sc9 - HYDROXYNITRILE LYASE FROM HEVEA BRASILIENSIS IN COMPLEX WITH THENATURAL SUBSTRATE ACETONE CYANOHYDRIN (Resolution = 1.80 Å).

Catalytic CATH Codes:

Display structure information

Overall Reaction:

Image of 2-hydroxy-2-methylpropanenitrile

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Image of Acetone

Image of Hydrogen cyanide

2-hydroxy-2-methylpropanenitrile
C02659
CHEBI:15348
Acetone
C00207
CHEBI:15347
Hydrogen cyanide
C01326
CHEBI:18407

Overall Comment: There is no evidence that the mechanism of the H. brasiliensis enzyme differs from that of the Manihot esculenta enzyme, although their substrate specificity is slightly different. The enzyme from H. brasiliensis tolerates aliphatic (including alpha,beta-unsaturated), aromatic and heterocyclic aldehydes, whereas the enzyme from M. esculenta catalyses the addition of hydrogen cyanide to aliphatic, aromatic, heteroaromatic aldehydes and methyl ketones. Both are specific to the S enantiomer. The overall reaction catalysed is very reversible and of importance to synthetic organic chemists.


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Stepwise Description of the Reaction

Step 1His235 (which is present as part of a Ser-His-Asp triad) deprotonates Ser70, deprotonates the hydroxide of the nitrile, initiating an elimination of the cyanate ion.
Step 2The cyanate ion deprotonates His235.

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
Asp 207 A Side Chain
His 235 A Side Chain
Ser 70 A Side Chain
Lys 236 A Side Chain
Thr 11 A Side Chain

References

  1. K.Gruber et al. (2004), J. Biol. Chem., 279, 20501-20510. Reaction mechanism of hydroxynitrile lyases of the alpha/beta-hydrolase superfamily: the three-dimensional structure of the transient enzyme-substrate complex certifies the crucial role of LYS236.
    Medline: 14998991

Homologue information for M0217 (1sc9)

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
0.26820.4252Compare
M0218 triacylglycerol lipase
3.1.1.3
1hpl 3.40.50.1820
0.29030.4074Compare
M0169 dipeptidyl-peptidase IV
3.4.14.5
1pfq 3.40.50.1820
0.27270.2999Compare
M0005 carboxypeptidase D
3.4.16.6
1whs 3.40.50.1820
0.27270.3856Compare

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

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lyase activity (molecular function)
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