Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

[Candida] boidinii

ABSTRACT: [Candida] boidinii Genome sequencing and assembly

PROVIDER: PRJNA359406 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	MSRX01.dat.gz	Other
	MSRX01.fasta.gz	Fasta.gz
	MSRX01.master.dat	Other
	MSRY01.dat.gz	Other
	MSRY01.fasta.gz	Fasta.gz

Items per page:

1 - 5 of 32

Similar Datasets

[Candida] boidinii

Project description:Candida boidinii overview

| PRJNA313990 | ENA

[Candida] boidinii

Project description:NBRP: Genome sequencing of Candida boidinii JCM 9604

| PRJDB3623 | ENA

[Candida] boidinii isolate:Y01308

Project description:[Candida] boidinii isolate:Y01308 Genome sequencing and assembly

| PRJNA427163 | ENA

[Candida] boidinii strain:GF002

Project description:De novo assembly of Candida boidinii genome

| PRJNA299882 | ENA

[Candida] boidinii strain:CICC#33029

Project description:[Candida] boidinii strain:CICC#33029 Genome sequencing

| PRJNA1089376 | ENA

[Candida] boidinii strain:Phaff 70-104

Project description:Candida boidinii Phaff 70-104 Standard Draft genome sequencing

| PRJNA346870 | ENA

Expression analysis of Candida glabrata CBS138 delta-vph2 mutant

Project description:Investigation of whole genome gene expression level changes in Candida glabrata CBS138 delta-vph2 mutant, compared to the wild-type strain in SC broth (pH5.0 and pH7.4). VPH2 gene encodes a protein that is the assembly factor of a functional V-ATPase. Loss of Vph2p leads to loss of a functional V-ATPase enzyme complex.

2016-08-09 | GSE66984 | GEO

Whole genome sequencing of Candida albicans tunicamycin adaptors

Project description:We used Candida albicans lab strain SC5314 to obtain tunicamycin adaptors. We did whole genome sequencing of the adaptors and the parent as well.

2021-04-24 | E-MTAB-10358 | biostudies-arrayexpress

Candida

Project description:Clinical isolates Candida Genome sequencing and assembly

| PRJNA1077920 | ENA

High-resolution structures of formate dehydrogenase from Candida boidinii.

Project description:The understanding of the mechanism of enzymatic recovery of NADH is of biological and of considerable biotechnological interest, since the essential, but expensive, cofactor NADH is exhausted in asymmetric hydrogenation processes, but can be recovered by NAD(+)-dependent formate dehydrogenase (FDH). Most accepted for this purpose is the FDH from the yeast Candida boidinii (CbFDH), which, having relatively low thermostability and specific activity, has been targeted by enzyme engineering for several years. Optimization by mutagenesis studies was performed based on physiological studies and structure modeling. However, X-ray structural information has been required in order to clarify the enzymatic mechanism and to enhance the effectiveness and operational stability of enzymatic cofactor regenerators in biocatalytic enantiomer synthesis as well as to explain the observed biochemical differences between yeast and bacterial FDH. We designed two single-point mutants in CbFDH using an adapted surface engineering approach, and this allowed crystals suitable for high-resolution X-ray structural studies to be obtained. The mutations improved the crystallizability of the protein and also the catalytic properties and the stability of the enzyme. With these crystal structures, we explain the observed differences from both sources, and form the basis for further rational mutagenesis studies.

| S-EPMC2206666 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data