KEGG   ENZYME: 1.16.1.8Help
Entry
EC 1.16.1.8                 Enzyme                                 

Name
[methionine synthase] reductase;
methionine synthase cob(II)alamin reductase (methylating);
methionine synthase reductase;
[methionine synthase]-cobalamin methyltransferase (cob(II)alamin reducing)
Class
Oxidoreductases;
Oxidizing metal ions;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
[methionine synthase]-methylcob(I)alamin,S-adenosylhomocysteine:NADP+ oxidoreductase
Reaction(IUBMB)
2 [methionine synthase]-methylcob(I)alamin + 2 S-adenosylhomocysteine + NADP+ = 2 [methionine synthase]-cob(II)alamin + NADPH + H+ + 2 S-adenosyl-L-methionine [RN:R05182]
Reaction(KEGG)
Substrate
[methionine synthase]-methylcob(I)alamin [CPD:C06410];
S-adenosylhomocysteine [CPD:C00021];
NADP+ [CPD:C00006]
Product
[methionine synthase]-cob(II)alamin [CPD:C06409];
NADPH [CPD:C00005];
H+ [CPD:C00080];
S-adenosyl-L-methionine [CPD:C00019]
Comment
In humans, the enzyme is a flavoprotein containing FAD and FMN. The substrate of the enzyme is the inactivated [Co(II)] form of EC 2.1.1.13, methionine synthase. Electrons are transferred from NADPH to FAD to FMN. Defects in this enzyme lead to hereditary hyperhomocysteinemia.
History
EC 1.16.1.8 created 1999 as EC 2.1.1.135, transferred 2003 to EC 1.16.1.8
Orthology
K00597  
[methionine synthase] reductase
Genes
HSA: 
4552(MTRR)
PTR: 
461717(MTRR)
PPS: 
100990677(MTRR)
GGO: 
101138335(MTRR)
PON: 
100174319(MTRR)
MCC: 
100430789(MTRR)
MCF: 
MMU: 
210009(Mtrr)
RNO: 
290947(Mtrr)
CGE: 
HGL: 
101720530(Mtrr)
TUP: 
102491380(MTRR)
CFA: 
478623(MTRR)
AML: 
100484655(MTRR)
FCA: 
101098359(MTRR)
BTA: 
507991(MTRR)
BOM: 
102272980(MTRR)
PHD: 
102327187(MTRR)
CHX: 
102171193(MTRR)
SSC: 
100516580(MTRR)
CFR: 
102511463(MTRR)
ECB: 
100071310(MTRR)
MYB: 
102241177(MTRR)
MDO: 
100013254(MTRR)
SHR: 
100923220(MTRR)
OAA: 
100089744(MTRR)
GGA: 
428502(MTRR)
MGP: 
TGU: 
100228556(MTRR)
FAB: 
101807366(MTRR)
PHI: 
102113343(MTRR)
APLA: 
101802959(MTRR)
FPG: 
101910301(MTRR)
FCH: 
102047448(MTRR)
CLV: 
102096989(MTRR)
ASN: 
102383326(MTRR)
PSS: 
102457990(MTRR)
ACS: 
100563923(mtrr)
XTR: 
733716(mtrr)
DRE: 
560667(mtrr)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
102351804(MTRR)
BFO: 
CIN: 
SPU: 
DME: 
DAN: 
DER: 
DWI: 
DGR: 
AGA: 
AAG: 
TCA: 
BMOR: 
PHU: 
ISC: 
CEL: 
CELE_C01G6.6(mtrr-1)
CBR: 
CBG00882(Cbr-tag-165)
BMY: 
LOA: 
TSP: 
SMM: 
NVE: 
HMG: 
TAD: 
AQU: 
GSL: 
CCP: 
MBR: 
DDI: 
DPP: 
DFA: 
PIF: 
GTT: 
NGR: 
 » show all
Taxonomy
Reference
1  [PMID:9501215]
  Authors
Leclerc D, Wilson A, Dumas R, Gafuik C, Song D, Watkins D, Heng HH, Rommens JM, Scherer SW, Rosenblatt DS, Gravel RA.
  Title
Cloning and mapping of a cDNA for methionine synthase reductase, a flavoprotein defective in patients with homocystinuria.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 3059-64.
  Organism
Homo sapiens [GN:hsa]
  Sequence
[hsa:4552]
Reference
2  [PMID:11466310]
  Authors
Olteanu H, Banerjee R.
  Title
Human methionine synthase reductase, a soluble P-450 reductase-like dual flavoprotein, is sufficient for NADPH-dependent methionine synthase activation.
  Journal
J. Biol. Chem. 276 (2001) 35558-63.
  Organism
Homo sapiens [GN:hsa]
Reference
3  [PMID:12416982]
  Authors
Olteanu H, Munson T, Banerjee R.
  Title
Differences in the efficiency of reductive activation of methionine synthase and exogenous electron acceptors between the common polymorphic variants of human methionine synthase reductase.
  Journal
Biochemistry. 41 (2002) 13378-85.
  Organism
Homo sapiens [GN:hsa]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
207004-87-3

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