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)
NLE: 100605425(MTRR)
MCC: 100430789(MTRR)
MCF: 101925754(MTRR)
CSAB: 103214983(MTRR)
RRO: 104674086(MTRR)
RBB: 108536959(MTRR)
CJC: 100389974(MTRR)
SBQ: 101042701(MTRR)
MMU: 210009(Mtrr)
RNO: 290947(Mtrr)
CGE: 100773236(Mtrr)
NGI: 103735353(Mtrr)
HGL: 101720530(Mtrr)
CCAN: 109688199(Mtrr)
OCU: 100350605(MTRR)
TUP: 102491380(MTRR)
CFA: 478623(MTRR)
AML: 100484655(MTRR)
UMR: 103662251(MTRR)
ORO: 101366274(MTRR)
FCA: 101098359(MTRR)
PTG: 102949230(MTRR)
AJU: 106971266(MTRR)
BTA: 507991(MTRR)
BOM: 102272980(MTRR)
BIU: 109574962(MTRR)
PHD: 102327187(MTRR)
CHX: 102171193(MTRR)
OAS: 101123409(MTRR)
SSC: 100516580(MTRR)
CFR: 102511463(MTRR)
CDK: 105094043(MTRR)
BACU: 103019188(MTRR)
LVE: 103085843(MTRR)
OOR: 101285453(MTRR)
ECB: 100071310(MTRR)
EPZ: 103540506(MTRR)
EAI: 106823000(MTRR)
MYB: 102241177(MTRR)
MYD: 102763596(MTRR)
RSS: 109453576(MTRR)
PALE: 102892778(MTRR)
LAV: 100654114(MTRR)
TMU: 101359820
MDO: 100013254(MTRR)
SHR: 100923220(MTRR)
OAA: 100089744(MTRR)
GGA: 428502(MTRR)
MGP: 100540427(MTRR)
CJO: 107309523(MTRR)
APLA: 101802959(MTRR)
ACYG: 106036580(MTRR)
TGU: 100228556(MTRR)
GFR: 102038689(MTRR)
FAB: 101807366(MTRR)
PHI: 102113343(MTRR)
PMAJ: 107200311(MTRR)
CCAE: 111925671(MTRR)
CCW: 104685872(MTRR)
FPG: 101910301(MTRR)
FCH: 102047448(MTRR)
CLV: 102096989(MTRR)
EGZ: 104126205(MTRR)
AAM: 106492684(MTRR)
ASN: 102383326(MTRR)
AMJ: 102561574(MTRR)
PSS: 102457990(MTRR)
CMY: 102929534(MTRR)
CPIC: 101951331(MTRR)
ACS: 100563923(mtrr)
PVT: 110089599(MTRR)
PBI: 103051443 103055371(MTRR)
GJA: 107108830(MTRR)
XLA: 108719055(mtrr.L)
XTR: 733716(mtrr)
NPR: 108802102(MTRR)
DRE: 560667(mtrr)
SANH: 107686717(mtrr) 107695375
SGH: 107549192 107595114(mtrr)
IPU: 108256395(mtrr)
AMEX: 103046907(mtrr)
TRU: 101070210(mtrr)
LCO: 104921714(mtrr)
NCC: 104954888(mtrr)
MZE: 101481719(mtrr)
OLA: 101167253(mtrr)
XMA: 102232227(mtrr)
PRET: 103482452(mtrr)
NFU: 107382941(mtrr)
KMR: 108243160(mtrr)
CSEM: 103377015(mtrr)
LCF: 108902055(mtrr)
SDU: 111237220(mtrr)
HCQ: 109511817(mtrr)
BPEC: 110160921(mtrr)
MALB: 109965535(mtrr)
ELS: 105019455(mtrr)
SFM: 108935528(mtrr)
LCM: 102351804(MTRR)
CMK: 103186339(mtrr)
CIN: 100182690
SPU: 581957
APLC: 110975926
SKO: 100371498
DME: Dmel_CG14882(CG14882)
DSI: Dsimw501_GD19100(Dsim_GD19100)
MDE: 101896273
TCA: 655238
DPA: 109546268
NVL: 108558885
BMOR: 101743356
PMAC: 106717667
HAW: 110376093
CLEC: 106670593
ZNE: 110830537
FCD: 110845930
TUT: 107363566
CEL: CELE_C01G6.6(mtrr-1)
CBR: CBG00882(Cbr-tag-165)
BMY: Bm1_35655
TSP: Tsp_01287
CRG: 105333103
OBI: 106882104
SHX: MS3_02917
EGL: EGR_00462
EPA: 110247156
ADF: 107342874
HMG: 100207049
AQU: 100635303
SPAR: SPRG_03729
NGR: NAEGRDRAFT_59563(FM177)
 » 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 95:3059-64 (1998)
DOI:10.1073/pnas.95.6.3059
  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 276:35558-63 (2001)
DOI:10.1074/jbc.M103707200
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 41:13378-85 (2002)
DOI:10.1021/bi020536s
Other DBs
ExplorEnz - The Enzyme Database: 1.16.1.8
IUBMB Enzyme Nomenclature: 1.16.1.8
ExPASy - ENZYME nomenclature database: 1.16.1.8
BRENDA, the Enzyme Database: 1.16.1.8
CAS: 207004-87-3

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