about
Betaine-homocysteine S-methyltransferase-2 is an S-methylmethionine-homocysteine methyltransferaseEvolutionary Analyses and Natural Selection of Betaine-Homocysteine S-Methyltransferase (BHMT) and BHMT2 GenesMetal active site elasticity linked to activation of homocysteine in methionine synthasesInsights into the reactivation of cobalamin-dependent methionine synthaseStructural basis for substrate activation and regulation by cystathionine beta-synthase (CBS) domains in cystathionine -synthaseStructural Basis of Multifunctionality in a Vitamin B12-processing EnzymeMitochondrial ribonuclease P structure provides insight into the evolution of catalytic strategies for precursor-tRNA 5' processingAutoinhibition and Signaling by the Switch II Motif in the G-protein Chaperone of a Radical B12 EnzymeSpecific potassium ion interactions facilitate homocysteine binding to betaine-homocysteine S-methyltransferaseStructure of Human B12 Trafficking Protein CblD Reveals Molecular Mimicry and Identifies a New Subfamily of Nitro-FMN ReductasesNuclear Protein-Only Ribonuclease P2 Structure and Biochemical Characterization Provide Insight into the Conserved Properties of tRNA 5' End Processing Enzymes.Differential substrate recognition by isozymes of plant protein-only Ribonuclease PSplicing variants of the porcine betaine-homocysteine S-methyltransferase gene: implications for mammalian metabolism.Loss of the mitochondrial protein-only ribonuclease P complex causes aberrant tRNA processing and lethality in Drosophila.RNase P enzymes: divergent scaffolds for a conserved biological reaction.Normal-mode analysis of FeCl4- and Fe2S2Cl42- via vibrational mössbauer, resonance Raman, and FT-IR spectroscopies.Dynamics of an [Fe4S4(SPh)4]2- cluster explored via IR, Raman, and nuclear resonance vibrational spectroscopy (NRVS)-analysis using 36S substitution, DFT calculations, and empirical force fields.Molecular recognition of pre-tRNA by Arabidopsis protein-only Ribonuclease P.Antivitamin B12 Inhibition of the Human B12 -Processing Enzyme CblC: Crystal Structure of an Inactive Ternary Complex with Glutathione as the Cosubstrate.The folate-binding module of Thermus thermophilus cobalamin-dependent methionine synthase displays a distinct variation of the classical TIM barrel: a TIM barrel with a `twist'.Rational synthesis of high nuclearity Mo/Fe/S clusters: the reductive coupling approach in the convenient synthesis of (Cl(4)-cat)(2)Mo(2)Fe(6)S(8)(PR(3))(6) [R = Et, (n)Pr, (n)Bu] and the new [(Cl(4)-cat)(2)Mo(2)Fe(2)S(3)O(PEt(3))(3)Cl]-1/2(Fe(PEt(Superclusters: a host-guest complex with a cyclic array of three bridged MoFe3S4 clustersMetal clusters as ligands: substitution of Fe ions in Fe/Mo/S clusters by thiophilic Cu(I) ions to give clusters with [Cu4Mo2Fe2S8]4+ and [Cu5Mo3Fe4S11]6+ coresSystematic synthesis of heterometallic Ni/Fe/S and Cu/Fe/S clusters with a pentlandite-like M8S6 coreMetal clusters as ligands. Substitution of fe ions in Fe/Mo/S clusters by thiophilic CuI ionsBorohydride, azide, and chloride anions as terminal ligands on Fe/Mo/S clusters. Synthesis, structure and characterization of [(Cl4-cat)(PPr3) MoFe3S4(X)2]2(Bu4N)4 and [(Cl4-cat)(PPr3)MoFe3S4 (PPr3)(X)]2(Bu4N)2 (X = N3-, BH4-, Cl-) double-fused cubaItaconyl-CoA forms a stable biradical in methylmalonyl-CoA mutase and derails its activity and repair
P50
Q24308183-28510CBC-FDC6-4E0C-A08C-704EAA8E828CQ27301531-1300BECE-5125-4E31-B2E0-9EE2E5958063Q27649929-EE496BEB-5011-46CC-B5E4-DA101F57A60EQ27657891-41B2BB40-7FD7-4118-9B90-1765DB36AC1FQ27665916-2309B69F-C61D-4F6F-90AF-30DBF418A3B9Q27670518-5190F9EB-CB91-4FBC-AB8A-6F07DB8E2CD9Q27673406-8C089628-C3C2-459E-A29F-9D724A2F472BQ27679846-750D441B-CF93-4053-B744-52A6844C035CQ27690648-4B2DBC86-A267-4E87-A9C2-9F152EF58AF9Q36443993-A1602313-E764-4DBC-9CF0-D2FCA4299155Q36535471-C23D21F7-4CAB-497F-86F3-0F5615351566Q36812738-E13A4CA6-26D9-4A05-837F-6109037DAA47Q37489529-B30EF276-6ECB-4CCD-8472-9B8E1CF5B887Q37623742-EE69DDFA-4145-4F28-BCD4-CFECCED27475Q41895901-A925F317-7437-45D9-98E9-6186E15069CEQ43584543-A15D481F-AC15-4129-BCE3-1D39AF816030Q45933184-B9CE8D3C-AC48-41A4-9E58-584C6DFE068DQ47852259-027D879C-16F7-49D3-9F75-A3CE8CF46D7DQ48095762-D7B66DE0-A109-4A27-B4EA-35A2E7E8368CQ48159985-FD5AEC7E-2183-4203-991F-49F5F9D0251CQ77078371-EEDA599D-9DA5-4B23-AE45-240BC076E1C5Q80598359-37E89EBC-B219-462D-BAD2-A4E58A8A45B7Q81426381-2E3B8ACA-0B6C-4BC8-816E-AA15DDAFE5DAQ81531124-68C7CF4B-8439-451D-83D2-7CD892746102Q82528159-C3F88CD4-73A7-45FF-A5F4-6DF8C59D5E7AQ83193007-ADF6242D-29B6-49FF-A260-0CF09C83F9EEQ91044260-03A4D5F9-4169-4D5F-9965-313AAF2B24C0
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Markos Koutmos
@ast
Markos Koutmos
@en
Markos Koutmos
@es
Markos Koutmos
@nl
type
label
Markos Koutmos
@ast
Markos Koutmos
@en
Markos Koutmos
@es
Markos Koutmos
@nl
prefLabel
Markos Koutmos
@ast
Markos Koutmos
@en
Markos Koutmos
@es
Markos Koutmos
@nl
P106
P31
P496
0000-0003-0933-6312