Evidence that pyridoxal phosphate modification of lysine residues (Lys-55 and Lys-59) causes inactivation of hydroxymethylbilane synthase (porphobilinogen deaminase).
about
Studies on the mechanism of hydroxymethylbilane synthase concerning the role of arginine residues in substrate bindingTwo different point G to A mutations in exon 10 of the porphobilinogen deaminase gene are responsible for acute intermittent porphyriaUnique properties of Plasmodium falciparum porphobilinogen deaminaseFunctions of the gene products of Escherichia coli.Investigation of putative active-site lysine residues in hydroxymethylbilane synthase. Preparation and characterization of mutants in which (a) Lys-55, (b) Lys-59 and (c) both Lys-55 and Lys-59 have been replaced by glutamine.
P2860
Evidence that pyridoxal phosphate modification of lysine residues (Lys-55 and Lys-59) causes inactivation of hydroxymethylbilane synthase (porphobilinogen deaminase).
description
1989 nî lūn-bûn
@nan
1989 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Evidence that pyridoxal phosph ...... e (porphobilinogen deaminase).
@ast
Evidence that pyridoxal phosph ...... e (porphobilinogen deaminase).
@en
type
label
Evidence that pyridoxal phosph ...... e (porphobilinogen deaminase).
@ast
Evidence that pyridoxal phosph ...... e (porphobilinogen deaminase).
@en
prefLabel
Evidence that pyridoxal phosph ...... e (porphobilinogen deaminase).
@ast
Evidence that pyridoxal phosph ...... e (porphobilinogen deaminase).
@en
P2093
P2860
P356
P1433
P1476
Evidence that pyridoxal phosph ...... e (porphobilinogen deaminase).
@en
P2093
A D Miller
A R Battersby
L C Packman
P R Alefounder
P2860
P304
P356
10.1042/BJ2620119
P407
P577
1989-08-01T00:00:00Z