Cytochrome P450–redox partner fusion enzymes

AW Munro, HM Girvan, KJ McLean - Biochimica et Biophysica Acta (BBA) …, 2007 - Elsevier
The cytochromes P450 (P450s) are a broad class of heme b-containing mono-oxygenase
enzymes. The vast majority of P450s catalyse reductive scission of molecular oxygen using …

Causes and consequences of impaired methionine synthase activity in acquired and inherited disorders of vitamin B12 metabolism

JL Guéant, RM Guéant-Rodriguez… - Critical reviews in …, 2022 - Taylor & Francis
Abstract Methyl-Cobalamin (Cbl) derives from dietary vitamin B12 and acts as a cofactor of
methionine synthase (MS) in mammals. MS encoded by MTR catalyzes the remethylation of …

The complex machinery of human cobalamin metabolism

TJ McCorvie, D Ferreira, WW Yue… - Journal of Inherited …, 2023 - Wiley Online Library
Abstract Vitamin B12 (cobalamin, Cbl) is required as a cofactor by two human enzymes, 5‐
methyltetrahydrofolate‐homocysteine methyltransferase (MTR) and methylmalonyl‐CoA …

Human methionine synthase reductase is a molecular chaperone for human methionine synthase

K Yamada, RA Gravel, T Toraya… - Proceedings of the …, 2006 - National Acad Sciences
Sustained activity of mammalian methionine synthase (MS) requires MS reductase (MSR),
but there have been few studies of the interactions between these two proteins. In this study …

[HTML][HTML] Molecular mechanism of metabolic NAD (P) H-dependent electron-transfer systems: The role of redox cofactors

T Iyanagi - Biochimica et Biophysica Acta (BBA)-Bioenergetics, 2019 - Elsevier
Abstract NAD (P) H-dependent electron-transfer (ET) systems require three functional
components: a flavin-containing NAD (P) H-dehydrogenase, one-electron carrier and metal …

Protein interactions in the human methionine synthase− methionine synthase reductase complex and implications for the mechanism of enzyme reactivation

KR Wolthers, NS Scrutton - Biochemistry, 2007 - ACS Publications
Methionine synthase (MS) is a cobalamin-dependent enzyme. It transfers a methyl group
from methyltetrahydrofolate to homocysteine forming methionine and tetrahydrofolate. On …

Versatile enzymology and heterogeneous phenotypes in cobalamin complementation type C disease

AJ Esser, S Mukherjee, IA Dereven'kov, SV Makarov… - Iscience, 2022 - cell.com
Nutritional deficiency and genetic errors that impair the transport, absorption, and utilization
of vitamin B 12 (B 12) lead to hematological and neurological manifestations. The cblC …

Switching pyridine nucleotide specificity in P450 BM3: mechanistic analysis of the W1046H and W1046A enzymes

R Neeli, O Roitel, NS Scrutton, AW Munro - Journal of Biological Chemistry, 2005 - ASBMB
Flavocytochrome P450 BM3 is a member of the diflavin reductase enzyme family. Members
include cytochrome P450 reductase, nitric-oxide synthase, methionine synthase reductase …

Kinetic and thermodynamic characterization of the common polymorphic variants of human methionine synthase reductase

H Olteanu, KR Wolthers, AW Munro, NS Scrutton… - Biochemistry, 2004 - ACS Publications
Human methionine synthase reductase (MSR) is a protein containing both FAD and FMN,
and it reactivates methionine synthase that has lost activity due to oxidation of cob (I) alamin …

Investigation on the interaction of riboflavin with aquacobalamin (Vitamin B12): A fluorescence quenching study

HA Hassanin - Journal of Photochemistry and Photobiology A …, 2022 - Elsevier
The interaction between two members of the vitamin B group, vitamin B 2 (Riboflavin, Rib)
and vitamin B 12 (aquacobalamin, H 2 OCbl), was investigated in an aqueous solution by …