The apparent malate synthase activity of Rhodobacter sphaeroides is due to two paralogous enzymes, (3S)-Malyl-coenzyme A (CoA)/{beta}-methylmalyl-CoA lyase and (3S)- Malyl-CoA thioesterase

The apparent malate synthase activity of Rhodobacter sphaeroides is due to two paralogous enzymes, (3S)-Malyl-coenzyme A (CoA)/{beta}-methylmalyl-CoA lyase and (3S)- Malyl-CoA thioesterase

Item
http://www.wikidata.org/entity/Q28489527
CLYBL is a polymorphic human enzyme with malate synthase and β-methylmalate synthase activityThe crystal structures of the tri-functional Chloroflexus aurantiacus and bi-functional Rhodobacter sphaeroides malyl-CoA lyases and comparison with CitE-like superfamily enzymes and malate synthasesiRsp1095: a genome-scale reconstruction of the Rhodobacter sphaeroides metabolic networkMethanol assimilation in Methylobacterium extorquens AM1: demonstration of all enzymes and their regulation.Metabolic and evolutionary insights into the closely-related species Streptomyces coelicolor and Streptomyces lividans deduced from high-resolution comparative genomic hybridization.A methylaspartate cycle in haloarchaea.Genome-scale reconstruction and system level investigation of the metabolic network of Methylobacterium extorquens AM1.Coassimilation of organic substrates via the autotrophic 3-hydroxypropionate bi-cycle in Chloroflexus aurantiacusThe ethylmalonyl-CoA pathway is used in place of the glyoxylate cycle by Methylobacterium extorquens AM1 during growth on acetate.Modularity of methylotrophy, revisited.Carboxylases in natural and synthetic microbial pathwaysA synthetic pathway for the fixation of carbon dioxide in vitro.Malate Synthase and β-Methylmalyl Coenzyme A Lyase Reactions in the Methylaspartate Cycle in Haloarcula hispanica.Oxalyl-coenzyme A reduction to glyoxylate is the preferred route of oxalate assimilation in Methylobacterium extorquens AM1.DLocalMotif: a discriminative approach for discovering local motifs in protein sequences.Structure of Methylobacterium extorquens malyl-CoA lyase: CoA-substrate binding correlates with domain shift.Biosynthesis of the Carbonylmethylene Structure Found in the Ketomemicin Class of Pseudotripeptides.
P2860

The apparent malate synthase activity of Rhodobacter sphaeroides is due to two paralogous enzymes, (3S)-Malyl-coenzyme A (CoA)/{beta}-methylmalyl-CoA lyase and (3S)- Malyl-CoA thioesterase

Item
http://www.wikidata.org/entity/Q28489527
description
2010 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մարտին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2010
@ast
im März 2010 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2010/03/01)
@sk
vědecký článek publikovaný v roce 2010
@cs
wetenschappelijk artikel (gepubliceerd op 2010/03/01)
@nl
наукова стаття, опублікована в березні 2010
@uk
مقالة علمية (نشرت في مارس 2010)
@ar
name
The apparent malate synthase a ...... d (3S)- Malyl-CoA thioesterase
@ast
The apparent malate synthase a ...... d (3S)- Malyl-CoA thioesterase
@en
The apparent malate synthase a ...... d (3S)- Malyl-CoA thioesterase
@nl
type
label
The apparent malate synthase a ...... d (3S)- Malyl-CoA thioesterase
@ast
The apparent malate synthase a ...... d (3S)- Malyl-CoA thioesterase
@en
The apparent malate synthase a ...... d (3S)- Malyl-CoA thioesterase
@nl
prefLabel
The apparent malate synthase a ...... d (3S)- Malyl-CoA thioesterase
@ast
The apparent malate synthase a ...... d (3S)- Malyl-CoA thioesterase
@en
The apparent malate synthase a ...... d (3S)- Malyl-CoA thioesterase
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P921
P932
P356
P1433
P1476
The apparent malate synthase a ...... d (3S)- Malyl-CoA thioesterase
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P921
P932