Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Homo sapiens

ABSTRACT: Gut Microbiota in Pregnant Malaysian Women

PROVIDER: PRJNA788699 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR17235400.fastq.gz	Fastqsanger.gz
	SRR17235401.fastq.gz	Fastqsanger.gz
	SRR17235402.fastq.gz	Fastqsanger.gz
	SRR17235403.fastq.gz	Fastqsanger.gz
	SRR17235404.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 76

Similar Datasets

homo sapiens

Project description:Gut microbiota of pregnant women with gestational diabetes.

| PRJNA884382 | ENA

Project description:gut microbiota of pregnant women

| PRJNA925813 | ENA

Project description:Gut microbiota of pregnant women

| PRJNA876635 | ENA

Project description:Gut microbiota of pregnant women

| PRJNA876087 | ENA

Project description:Gut microbiota of healthy pregnant women

| PRJNA975340 | ENA

Project description:Characteristics of gut microbiota associated with pregnant women

| PRJNA1165346 | ENA

Crystal structure of Homo sapiens kynureninase.

Project description:Kynureninase is a member of a large family of catalytically diverse but structurally homologous pyridoxal 5'-phosphate (PLP) dependent enzymes known as the aspartate aminotransferase superfamily or alpha-family. The Homo sapiens and other eukaryotic constitutive kynureninases preferentially catalyze the hydrolytic cleavage of 3-hydroxy-l-kynurenine to produce 3-hydroxyanthranilate and l-alanine, while l-kynurenine is the substrate of many prokaryotic inducible kynureninases. The human enzyme was cloned with an N-terminal hexahistidine tag, expressed, and purified from a bacterial expression system using Ni metal ion affinity chromatography. Kinetic characterization of the recombinant enzyme reveals classic Michaelis-Menten behavior, with a Km of 28.3 +/- 1.9 microM and a specific activity of 1.75 micromol min-1 mg-1 for 3-hydroxy-dl-kynurenine. Crystals of recombinant kynureninase that diffracted to 2.0 A were obtained, and the atomic structure of the PLP-bound holoenzyme was determined by molecular replacement using the Pseudomonas fluorescens kynureninase structure (PDB entry 1qz9) as the phasing model. A structural superposition with the P. fluorescens kynureninase revealed that these two structures resemble the "open" and "closed" conformations of aspartate aminotransferase. The comparison illustrates the dynamic nature of these proteins' small domains and reveals a role for Arg-434 similar to its role in other AAT alpha-family members. Docking of 3-hydroxy-l-kynurenine into the human kynureninase active site suggests that Asn-333 and His-102 are involved in substrate binding and molecular discrimination between inducible and constitutive kynureninase substrates.

| S-EPMC2531291 | biostudies-literature

Homo sapiens

Project description:Cell-free DNA sequencing of pregnant women

| PRJNA268876 | ENA