Literature summary for 4.2.1.127 extracted from

Nestl, B.M.; Geinitz, C.; Popa, S.; Rizek, S.; Haselbeck, R.J.; Stephen, R.; Noble, M.A.; Fischer, M.P.; Ralph, E.C.; Hau, H.T.; Man, H.; Omar, M.; Turkenburg, J.P.; van Dien, S.; Culler, S.J.; Grogan, G.; Hauer, B.
Structural and functional insights into asymmetric enzymatic dehydration of alkenols (2017), Nat. Chem. Biol., 13, 275-281 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
purified wild-type enzyme LinD alone or in complex with geraniol, or as selenomethionine-labeled enzyme, X-ray diffraction structure determination and analysis at 1.76-2.68 A resolution	Castellaniella defragrans

Protein Variants

Protein Variants	Comment	Organism
C171A	site-directed mutagenesis, inactive mutant	Castellaniella defragrans
C180A	site-directed mutagenesis, inactive mutant	Castellaniella defragrans
H129A	site-directed mutagenesis, the mutant shows 23% epimerase and 6% dehydratase, respectively, compared to the wild-type	Castellaniella defragrans
M125A	site-directed mutagenesis, the mutant shows 2% epimerase and no dehydratase, respectively, compared to the wild-type	Castellaniella defragrans
Y45F	site-directed mutagenesis, the mutant shows 22% epimerase and no dehydratase, respectively, compared to the wild-type	Castellaniella defragrans

Inhibitors

Inhibitors	Comment	Organism	Structure
linalyl amine	the simultaneous utilization of 10 mM (3S)-linalool and varying concentrations (0.01-10 mM) of linalyl amine in biotransformations results in almost complete inactixadvation (over 98%) of LinD even when the amine concentration is low	Castellaniella defragrans

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
(3S)-linalool	Castellaniella defragrans	-	beta-myrcene + H2O	-	r
additional information	Castellaniella defragrans	the bifunctional linalool dehydratase isomerase (LinD)catalyzes the isomerization of geraniol to linalool, EC 5.4.4.4, and likewise the dehydration of linalool to beta-myrcene, EC 4.2.1.127	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Castellaniella defragrans	E1XUJ2	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
(3S)-linalool = myrcene + H2O	reaction mechanism, overview	Castellaniella defragrans	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(3S)-linalool	-	Castellaniella defragrans	beta-myrcene + H2O	-	r
(6E)-3,7,11-trimethyldodeca-1,6,10-trien-3-ol	-	Castellaniella defragrans	(6E)-7,11-dimethyl-3-methylidenedodeca-1,6,10-triene + H2O	-	r
(E)-3-methylocta-1,4-dien-3-ol	-	Castellaniella defragrans	(4E)-3-methylideneocta-1,4-diene + H2O	-	r
(E/Z)-4,8-dimethylnona-2,7-dien-4-ol	-	Castellaniella defragrans	(7E)-2-methyl-6-methylidenenona-2,7-diene + H2O	-	r
2-methylbut-3-en-2-ol	-	Castellaniella defragrans	2-methylbuta-1,3-diene + H2O	-	r
3-ethyloct-1-en-3-ol	-	Castellaniella defragrans	(3E)-3-ethylidene-7-methylocta-1,6-diene + H2O	-	r
3-methoxy-3,7-dimethylocta-1,6-diene	-	Castellaniella defragrans	beta-myrcene	-	r
3-methyl-5-phenylpent-1-en-3-ol	-	Castellaniella defragrans	(3-methylidenepent-4-en-1-yl)benzene + H2O	-	r
3-methylhept-1-en-3-ol	-	Castellaniella defragrans	3-methylidenehept-1-ene + H2O	-	r
3-methylhex-1-en-3-ol	-	Castellaniella defragrans	3-methylidenehex-1-ene + H2O	-	r
additional information	the bifunctional linalool dehydratase isomerase (LinD)catalyzes the isomerization of geraniol to linalool, EC 5.4.4.4, and likewise the dehydration of linalool to beta-myrcene, EC 4.2.1.127	Castellaniella defragrans	?	-	?
additional information	enzyme LinD shows a broad substrate specificity, truncated and elongated aromatic and aliphatic tertiary alcohols (C5-C15) that contain a specific signature motif can be substrates, structural requirements for substrates, overview. GC/MS analysis of linalool methyl ether conversion with LinD. No dehydratase activity with 2,6-dimethylhept-5-en-2-ol, 3,7-dimethyloct-6-en-3-ol, (E)-3-methyloct-4-en-3-ol, (E)-3,7-dimethyl-1,4,6-trien-3-ol, (E)-3,7-dimethylocta-4,6-dien-3-ol, 7-methylocta-1,6-dien-3-ol, 3,7-dimethylocta-1,6-dien-3-amine (i.e. linalyl amine), and 3,7-dimethyloct-6-en-1-yn-3-ol. Compounds 3-methylbut-2-en-1-ol, (2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-ol, and geraniol are substrates for the isomerization activity of the enzyme	Castellaniella defragrans	?	-	?

Subunits

Subunits	Comment	Organism
?	x * 43000, recombinant wild-type enzyme, SDS-PAGE	Castellaniella defragrans

Synonyms

Synonyms	Comment	Organism
bifunctional linalool dehydratase isomerase	-	Castellaniella defragrans
LinD	-	Castellaniella defragrans
More	cf. EC 5.4.4.4	Castellaniella defragrans

General Information

General Information	Comment	Organism
additional information	structure of LinD in complex with the prodxaduct geraniol, structure-function relationship, overview. Cys171 is well positioned to protonate the linalool hydroxyl of the (S)-configuration, and a covalent LinD-terpene complex is formed as the hydroxyl is eliminated as water. The covalent intermediate underxadgoes either hydrolysis, by a water molecule activated by His129, to give geraniol in an isomerization reaction, or base-catalyzed elimixadnation, most likely by Asp39 or Tyr45 at the methyl group, to give myrcene in a dehydration process. In the second proposal, involvxading a carbocation intermediate, Cys180 does not interact directly with the substrate terminal C=C double bond. Dehydration of (3S)-linalool, catalyzed by Cys171, results in a carbocation intermediate that undergoes either rehydration, catalyzed by His129 or Cys180 to form geraniol, or base-catalyzed deprotonation to form myrcene by Tyr45 and Asp39	Castellaniella defragrans
physiological function	the bifunctional linalool dehydratase isomerase (LinD) from the bacterium Castellaniella defragrans catalyzes in nature the hydration of beta-myrcene to (3S)-linalool and the subsequent isomerization to geraniol	Castellaniella defragrans

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Release 2023.1 (January 2023)