Cloning, expression, and characterization of coenzyme-B₁₂-dependent diol dehydratase from Lactobacillus diolivorans
The three gldCDE genes from Lactobacillus diolivorans, that encode the three subunits of the glycerol dehydratase, were cloned and the proteins were co-expressed in soluble form in Escherichia coli with added sorbitol and betaine hydrochloride. The purified enzyme exists as a heterohexamer (α₂β₂γ₂)...
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| Published in | Biotechnology letters Vol. 36; no. 1; pp. 159 - 165 |
|---|---|
| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Dordrecht
Springer-Verlag
2014
Springer Netherlands |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0141-5492 1573-6776 1573-6776 |
| DOI | 10.1007/s10529-013-1346-8 |
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| Abstract | The three gldCDE genes from Lactobacillus diolivorans, that encode the three subunits of the glycerol dehydratase, were cloned and the proteins were co-expressed in soluble form in Escherichia coli with added sorbitol and betaine hydrochloride. The purified enzyme exists as a heterohexamer (α₂β₂γ₂) structure with a native molecular mass of 210 kDa. It requires coenzyme B₁₂ for catalytic activity and is subject to suicide inactivation by glycerol during catalysis. The enzyme had maximum activity at pH 8.6 and 37 °C. The apparent K ₘ values for coenzyme B₁₂, 1,2-ethanediol, 1,2-propanediol, and glycerol were 1.5 μM, 10.5 mM, 1.3 mM, and 5.8 mM, respectively. Together, these results indicated that the three genes gldCDE encoding the proteins make up a coenzyme B₁₂-dependent diol dehydratase and not a glycerol dehydratase. |
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| AbstractList | The three
gldCDE
genes from
Lactobacillus diolivorans
, that encode the three subunits of the glycerol dehydratase, were cloned and the proteins were co-expressed in soluble form in
Escherichia coli
with added sorbitol and betaine hydrochloride. The purified enzyme exists as a heterohexamer (α
2
β
2
γ
2
) structure with a native molecular mass of 210 kDa. It requires coenzyme B
12
for catalytic activity and is subject to suicide inactivation by glycerol during catalysis. The enzyme had maximum activity at pH 8.6 and 37 °C. The apparent
K
m
values for coenzyme B
12
, 1,2-ethanediol, 1,2-propanediol, and glycerol were 1.5 μM, 10.5 mM, 1.3 mM, and 5.8 mM, respectively. Together, these results indicated that the three genes
gldCDE
encoding the proteins make up a coenzyme B
12
-dependent diol dehydratase and not a glycerol dehydratase. The three gldCDE genes from Lactobacillus diolivorans, that encode the three subunits of the glycerol dehydratase, were cloned and the proteins were co-expressed in soluble form in Escherichia coli with added sorbitol and betaine hydrochloride. The purified enzyme exists as a heterohexamer (α2β2γ2) structure with a native molecular mass of 210 kDa. It requires coenzyme B12 for catalytic activity and is subject to suicide inactivation by glycerol during catalysis. The enzyme had maximum activity at pH 8.6 and 37 °C. The apparent K m values for coenzyme B12, 1,2-ethanediol, 1,2-propanediol, and glycerol were 1.5 μM, 10.5 mM, 1.3 mM, and 5.8 mM, respectively. Together, these results indicated that the three genes gldCDE encoding the proteins make up a coenzyme B12-dependent diol dehydratase and not a glycerol dehydratase.The three gldCDE genes from Lactobacillus diolivorans, that encode the three subunits of the glycerol dehydratase, were cloned and the proteins were co-expressed in soluble form in Escherichia coli with added sorbitol and betaine hydrochloride. The purified enzyme exists as a heterohexamer (α2β2γ2) structure with a native molecular mass of 210 kDa. It requires coenzyme B12 for catalytic activity and is subject to suicide inactivation by glycerol during catalysis. The enzyme had maximum activity at pH 8.6 and 37 °C. The apparent K m values for coenzyme B12, 1,2-ethanediol, 1,2-propanediol, and glycerol were 1.5 μM, 10.5 mM, 1.3 mM, and 5.8 mM, respectively. Together, these results indicated that the three genes gldCDE encoding the proteins make up a coenzyme B12-dependent diol dehydratase and not a glycerol dehydratase. The three gldCDE genes from Lactobacillus diolivorans, that encode the three subunits of the glycerol dehydratase, were cloned and the proteins were co-expressed in soluble form in Escherichia coli with added sorbitol and betaine hydrochloride. The purified enzyme exists as a heterohexamer (α₂β₂γ₂) structure with a native molecular mass of 210 kDa. It requires coenzyme B₁₂ for catalytic activity and is subject to suicide inactivation by glycerol during catalysis. The enzyme had maximum activity at pH 8.6 and 37 °C. The apparent K ₘ values for coenzyme B₁₂, 1,2-ethanediol, 1,2-propanediol, and glycerol were 1.5 μM, 10.5 mM, 1.3 mM, and 5.8 mM, respectively. Together, these results indicated that the three genes gldCDE encoding the proteins make up a coenzyme B₁₂-dependent diol dehydratase and not a glycerol dehydratase. The three gldCDE genes from Lactobacillus diolivorans, that encode the three subunits of the glycerol dehydratase, were cloned and the proteins were co-expressed in soluble form in Escherichia coli with added sorbitol and betaine hydrochloride. The purified enzyme exists as a heterohexamer (α2β2γ2) structure with a native molecular mass of 210 kDa. It requires coenzyme B12 for catalytic activity and is subject to suicide inactivation by glycerol during catalysis. The enzyme had maximum activity at pH 8.6 and 37 °C. The apparent K m values for coenzyme B12, 1,2-ethanediol, 1,2-propanediol, and glycerol were 1.5 μM, 10.5 mM, 1.3 mM, and 5.8 mM, respectively. Together, these results indicated that the three genes gldCDE encoding the proteins make up a coenzyme B12-dependent diol dehydratase and not a glycerol dehydratase. The three gldCDE genes from Lactobacillus diolivorans, that encode the three subunits of the glycerol dehydratase, were cloned and the proteins were co-expressed in soluble form in Escherichia coli with added sorbitol and betaine hydrochloride. The purified enzyme exists as a heterohexamer (α₂β₂γ₂) structure with a native molecular mass of 210 kDa. It requires coenzyme B₁₂for catalytic activity and is subject to suicide inactivation by glycerol during catalysis. The enzyme had maximum activity at pH 8.6 and 37 °C. The apparent Kₘvalues for coenzyme B₁₂, 1,2-ethanediol, 1,2-propanediol, and glycerol were 1.5 μM, 10.5 mM, 1.3 mM, and 5.8 mM, respectively. Together, these results indicated that the three genes gldCDE encoding the proteins make up a coenzyme B₁₂-dependent diol dehydratase and not a glycerol dehydratase. |
| Author | Du, Liqin Wei, Yutuo Meng, Xiaolei Chen, Yunlai Wei, Xuqin Huang, Ribo |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/24078133$$D View this record in MEDLINE/PubMed |
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| CitedBy_id | crossref_primary_10_1007_s10529_014_1670_7 crossref_primary_10_3390_synbio1010002 crossref_primary_10_3389_fbioe_2019_00124 crossref_primary_10_1007_s00775_016_1371_x crossref_primary_10_1007_s11157_016_9415_9 crossref_primary_10_1186_s13068_017_0982_y crossref_primary_10_1002_bit_28170 crossref_primary_10_1186_s13068_023_02427_8 |
| Cites_doi | 10.1007/s00203-008-0443-x 10.1007/BF00408381 10.1128/JB.05661-11 10.1271/bbb.62.1774 10.1006/abbi.1997.0325 10.1111/1574-6968.12168 10.1111/j.1574-6968.1998.tb13062.x 10.1111/j.1574-6976.1998.tb00387.x 10.1074/jbc.271.37.22352 10.1016/0014-5793(91)81372-F 10.1016/0006-291X(76)90546-5 10.1016/j.biortech.2012.05.121 10.1046/j.1432-1033.2002.03288.x 10.1074/jbc.270.13.7142 10.1046/j.1432-1327.2001.02123.x 10.1007/s00253-003-1497-y 10.1128/JB.141.3.1439-1442.1980 10.1128/JB.181.19.5967-5975.1999 10.1016/S0021-9258(18)96700-1 10.1016/S0021-9258(19)75192-8 10.1099/00207713-52-2-639 10.1128/jb.178.19.5793-5796.1996 10.1016/S0021-9258(19)67979-2 |
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| Keywords | Characterization Diol dehydratase Coenzyme B Expression dependent Glycerol dehydratase |
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| Snippet | The three gldCDE genes from Lactobacillus diolivorans, that encode the three subunits of the glycerol dehydratase, were cloned and the proteins were... The three gldCDE genes from Lactobacillus diolivorans , that encode the three subunits of the glycerol dehydratase, were cloned and the proteins were... |
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| SubjectTerms | Applied Microbiology Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism betaine Biochemistry Biomedical and Life Sciences Biotechnology catalytic activity Cloning, Molecular Cobamides enzyme inactivation Escherichia coli glycerol Glycerol - metabolism Lactobacillus Lactobacillus - enzymology Lactobacillus - genetics Life Sciences Microbiology molecular weight Original Research Paper Oxygen - metabolism Propanediol Dehydratase - chemistry Propanediol Dehydratase - genetics Propanediol Dehydratase - metabolism Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism sorbitol |
| Title | Cloning, expression, and characterization of coenzyme-B₁₂-dependent diol dehydratase from Lactobacillus diolivorans |
| URI | https://link.springer.com/article/10.1007/s10529-013-1346-8 https://www.ncbi.nlm.nih.gov/pubmed/24078133 https://www.proquest.com/docview/1501372934 https://www.proquest.com/docview/1524147885 |
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