A propionate CoA-transferase of Ralstonia eutropha H16 with broad substrate specificity catalyzing the CoA thioester formation of various carboxylic acids

We have cloned, overexpressed, purified, and characterized a 2-ketogluconate kinase (2-dehydrogluconokinase, EC 2.7.1.13) from Cupriavidus necator (Ralstonia eutropha) H16. Exploration of its substrate specificity revealed that three ketoacids (2-keto-3-deoxy-d-gluconate, 2-keto-d-gulonate, and 2-keto-3-deoxy-d-gulonate) with structures close to the natural substrate (2-keto-d-gluconate) were successfully phosphorylated at an efficiency lower than or comparable to 2-ketogluconate, as depicted by the measured kinetic constant values. Eleven aldo and keto monosaccharides of different chain lengths and stereochemistries were also assayed but not found to be substrates. 2-ketogluconate-6-phosphate was synthesized at a preparative scale and was fully characterized for the first time.

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Faculty Opinions recommendation of UDP-sugar pyrophosphorylase with broad substrate specificity toward various monosaccharide 1-phosphates from pea sprouts.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1021628.246636 ◽

2004 ◽

Author(s):

Christoph Benning

Keyword(s):

Substrate Specificity ◽

Broad Substrate Specificity

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Faculty Opinions recommendation of Spectroscopic insights into the oxygen-tolerant membrane-associated [NiFe] hydrogenase of Ralstonia eutropha H16.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1161373.621887 ◽

2009 ◽

Author(s):

Michael Maroney ◽

Crisjoe Joseph

Keyword(s):

Ralstonia Eutropha ◽

Ralstonia Eutropha H16

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Faculty Opinions recommendation of A rice family 9 glycoside hydrolase isozyme with broad substrate specificity for hemicelluloses in type II cell walls.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.722918335.793513580 ◽

2016 ◽

Author(s):

Daniel Cosgrove

Keyword(s):

Substrate Specificity ◽

Cell Walls ◽

Glycoside Hydrolase ◽

Type Ii ◽

Broad Substrate Specificity ◽

Type Ii Cell

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CbbR and RegA regulate cbb operon transcription in Ralstonia eutropha H16

Journal of Biotechnology ◽

10.1016/j.jbiotec.2017.07.005 ◽

2017 ◽

Vol 257 ◽

pp. 78-86 ◽

Cited By ~ 2

Author(s):

Steffen Gruber ◽

Helmut Schwab ◽

Petra Heidinger

Keyword(s):

Ralstonia Eutropha ◽

Ralstonia Eutropha H16

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Polyhydroxyalkanoate copolyesters produced by Ralstonia eutropha PHB−4 harboring a low-substrate-specificity PHA synthase PhaC2Ps from Pseudomonas stutzeri 1317

Biochemical Engineering Journal ◽

10.1016/j.bej.2006.10.005 ◽

2006 ◽

Vol 32 (3) ◽

pp. 218-225 ◽

Cited By ~ 32

Author(s):

Rongcong Luo ◽

Jingyu Chen ◽

Lei Zhang ◽

Guoqiang Chen

Keyword(s):

Substrate Specificity ◽

Ralstonia Eutropha ◽

Pseudomonas Stutzeri ◽

Pha Synthase

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LASS3 (longevity assurance homologue 3) is a mainly testis-specific (dihydro)ceramide synthase with relatively broad substrate specificity

Biochemical Journal ◽

10.1042/bj20060379 ◽

2006 ◽

Vol 398 (3) ◽

pp. 531-538 ◽

Cited By ~ 116

Author(s):

Yukiko Mizutani ◽

Akio Kihara ◽

Yasuyuki Igarashi

Keyword(s):

Amino Acid ◽

Substrate Specificity ◽

Family Members ◽

Fatty Acyl ◽

Ceramide Synthase ◽

Broad Substrate Specificity ◽

Acid Protein ◽

Amino Acid Protein

The LASS (longevity assurance homologue) family members are highly conserved from yeasts to mammals. Five mouse and human LASS family members, namely LASS1, LASS2, LASS4, LASS5 and LASS6, have been identified and characterized. In the present study we cloned two transcriptional variants of hitherto-uncharacterized mouse LASS3 cDNA, which encode a 384-amino-acid protein (LASS3) and a 419-amino-acid protein (LASS3-long). In vivo, [3H]dihydrosphingosine labelling and electrospray-ionization MS revealed that overproduction of either LASS3 isoform results in increases in several ceramide species, with some preference toward those having middle- to long-chain-fatty acyl-CoAs. A similar substrate preference was observed in an in vitro (dihydro)ceramide synthase assay. These results indicate that LASS3 possesses (dihydro)ceramide synthesis activity with relatively broad substrate specificity. We also found that, except for a weak display in skin, LASS3 mRNA expression is limited almost solely to testis, implying that LASS3 plays an important role in this gland.

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