HOME
login
history
all enzymes
BRENDA home
History
Information on EC 1.5.1.10 - saccharopine dehydrogenase (NADP+, L-glutamate-forming)
for references in articles please use BRENDA:EC1.5.1.10Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.5.1.10 saccharopine dehydrogenase (NADP+, L-glutamate-forming)Specify your search results
Word Map
- 1.5.1.10
- alpha-aminoadipate
-
auxotrophs
-
magnaporthe
- homocitrate
- grisea
-
pipecolic
-
unlinked
- homoisocitrate
-
penicillium
- swainsonine
-
alkaloid
-
piperideine-6-carboxylic
-
rossmann
- chrysogenum
-
all-helical
-
embedding
- oxytropis
-
ph-rate
-
gene-enzyme
-
anisotropic
-
endophytic
-
acid-base
-
6-dehydrogenase
- diaminopimelate
-
substrate-assisted
- dl-alpha-aminoadipate
- l-pipecolate
-
seven-stranded
-
leaky
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
saccharopine reductase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, saccharopine (nicotinamide adenine dinucleotide phosphate, glutamate-forming)
-
-
-
epsilon-N-(L-glutaryl-2)-L-lysine:NAD+(P) oxidoreductase (L-2-aminoadipate-semialdehyde forming)
-
-
-
saccharopine reductase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
-
-
-
-
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
ordered kinetic mechanism, the reduced dinucleotide substrate binds to enzyme first followed by L-alpha-aminoadipate-delta-semialdehyde, which adds in rapid equilibrium prior to L-glutamate, saccharopine is released prior to NADP+, primary deuterium kinetic isotope effects and solvent deuterium kinetic isotope effects, overview. A conformational change to open the site and release products (in the direction of saccharopine formation) is the rate limiting step. Two groups are involved in the acid-base chemistry of the reaction. An enzyme group with a pKa of 5.6 accepts a proton from the alpha-amine of glutamate to generate the neutral amine that can act as a nucleophile. The alpha-amine of glutamate attacks the carbonyl of the semialdehyde to generate the carbinolamine, which is protonated by a second enzyme group with a pKa of about 7.8-8.0. Ionizable residues that might play a role in the acid-base mechanism of the enzyme are D126, C154 and/or Y99
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
N6-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase (L-glutamate-forming)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9033-55-0
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH + H+
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
-
-
r
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
saccharopine + NADP+ + H2O
-
piperidine-6-carboxylic acid and alpha-aminoadipate are precursors for synthesis of alpha-aminoadipate 6-semialdehyde via 3 different pathways, penultimate step in L-lysine biosynthesis
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
-
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
saccharopine + NADP+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
-
reverse reaction direction used for activity assay, end product is piperidine-6-carboxylic acid in assays using cell extract
-
r
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
lysine biosynthesis
-
?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
lysine biosynthesis
-
?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
-
?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
-
-
r
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
-
-
r
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
-
N6-(L-1,3-dicarboxypropyl)-L-lysine is identical with saccharopine
r
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
-
N6-(L-1,3-dicarboxypropyl)-L-lysine is identical with saccharopine
r
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
-
N6-(L-1,3-dicarboxypropyl)-L-lysine is identical with saccharopine
r
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
lysine biosynthesis
-
?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
lysine biosynthesis
-
?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
lysine biosynthesis
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
-
-
r
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
enzyme catalyzes the penultimate step in lysine biosynthesis
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
saccharopine + NADP+ + H2O
-
piperidine-6-carboxylic acid and alpha-aminoadipate are precursors for synthesis of alpha-aminoadipate 6-semialdehyde via 3 different pathways, penultimate step in L-lysine biosynthesis
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + 2-aminoadipate 6-semialdehyde + NADPH + H+
enzyme catalyzes the penultimate step in lysine biosynthesis
-
-
?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
lysine biosynthesis
-
?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
lysine biosynthesis
-
?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
lysine biosynthesis
-
?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
lysine biosynthesis
-
?
2-aminoadipate 6-semialdehyde + L-glutamate + NADPH
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
lysine biosynthesis
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
-
-
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
NAD+ and NADP+ equally effective in 2-aminoadipate 6-semialdehyde formation
NADP+
-
NAD+ and NADP+ equally effective in 2-aminoadipate 6-semialdehyde formation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-amino-6-heptenoic acid
-
competitive inhibition versus L-alpha-aminoadipate-delta-semialdehyde, uncompetitive inhibition versus NADPH, and noncompetitive inhibtition versus L-glutamate
2-oxoglutarate
-
competitive inhibition versus L-glutamate and uncompetitive inhibition versus L-alpha-aminoadipate-delta-semialdehyde and NADPH; competitive inhibition versus saccharopine and uncompetitive inhibition versus NADP+
alpha-AASA
-
shows noncompetitive inhibition versus saccharopine and uncompetitive inhibition versus NADP+
glyoxylic acid
-
competitive inhibition versus saccharopine and uncompetitive inhibition versus NADP+
L-glutamate
-
exhibits noncompetitive inhibition versus NADP+ and saccharopine
L-ornithine
-
competitive inhibition versus saccharopine and uncompetitive inhibition versus NADP+
L-pipecolic acid
-
competitive inhibition versus saccharopine and uncompetitive inhibition versus NADP+
N-oxalylglycine
-
competitive inhibition versus saccharopine and uncompetitive inhibition versus NADP+
NADP+
-
competitive inhibition versus NADPH, noncompetitive inhibition versus L-alpha-aminoadipate-delta-semialdehyde and L-glutamate
saccharopine
-
exhibits noncompetitive inhibition against L-alpha-aminoadipate-delta-semialdehyde, L-glutamate, and NADPH
L-leucine
-
competitive inhibition versus saccharopine and uncompetitive inhibition versus NADP+
NADPH
-
inhibition is competitive versus NADP+ and noncompetitive versus saccharopine
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 7.8
-
pH 5.5: about 45% of activity maximum, pH 7.8: about 35% of activity maximum
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
serotype A, strain H99, human pathogen, chimeric spermidine synthase-saccharopine dehydrogenase gene (SPE3-LYS9)
SwissProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
saccharopine reductase catalyzes the reductive amination of L-alpha-aminoadipate-delta-semialdehyde with L-glutamate to give saccharopine
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SCPDH_DICDI
480
0
53359
Swiss-Prot
other Location (Reliability: 3)
LYS9_MAGO7
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)
450
0
49097
Swiss-Prot
other Location (Reliability: 5)
LYS9_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
450
0
49938
Swiss-Prot
other Location (Reliability: 5)
LYS9_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
446
0
48918
Swiss-Prot
Secretory Pathway (Reliability: 5)
M5BMG1_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
345
0
37919
TrEMBL
other Location (Reliability: 1)
G7V6N8_THELD
Thermovirga lienii (strain ATCC BAA-1197 / DSM 17291 / Cas60314)
440
0
48647
TrEMBL
-
B0CXB5_LACBS
Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686)
751
0
82177
TrEMBL
other Location (Reliability: 2)
C7RCP0_KANKD
Kangiella koreensis (strain DSM 16069 / KCTC 12182 / SW-125)
441
0
48272
TrEMBL
-
A0A3B0TCJ0_9ZZZZ
458
0
51870
TrEMBL
other Location (Reliability: 4)
A0A3B0S7L5_9ZZZZ
390
0
42645
TrEMBL
Secretory Pathway (Reliability: 4)
Q5V5J8_HALMA
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
429
0
46468
TrEMBL
-
A0A2G9GK14_9LAMI
464
0
50900
TrEMBL
Mitochondrion (Reliability: 3)
A0A1S8A5N8_ROSNE
414
0
45275
TrEMBL
Mitochondrion (Reliability: 5)
A0A0N1NES3_9ACTN
383
0
41016
TrEMBL
-
A0A0P7W451_9RHOB
375
0
41354
TrEMBL
-
A0A3B0TN80_9ZZZZ
433
0
49635
TrEMBL
other Location (Reliability: 1)
A0A3B0SJ10_9ZZZZ
379
0
42084
TrEMBL
other Location (Reliability: 4)
G0HW78_HALHT
Haloarcula hispanica (strain ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182 / NCIMB 2187 / VKM B-1755)
426
0
46388
TrEMBL
-
A0A3G2SB36_9BASI
763
0
83577
TrEMBL
other Location (Reliability: 3)
A0A3B0QUU6_9ZZZZ
454
0
51578
TrEMBL
other Location (Reliability: 3)
A3LQ43_PICST
Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545)
444
0
48567
TrEMBL
other Location (Reliability: 5)
A0A364MWU3_9PLEO
468
0
51218
TrEMBL
other Location (Reliability: 2)
A0A0J5TF32_9RHOB
379
0
41730
TrEMBL
-
A2QB21_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
462
0
49774
TrEMBL
Secretory Pathway (Reliability: 4)
G3Y9B4_ASPNA
Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7)
450
0
49357
TrEMBL
other Location (Reliability: 5)
A0A2S5BAT4_9BASI
750
0
81646
TrEMBL
other Location (Reliability: 2)
A0A3B1CAH0_9ZZZZ
237
0
26650
TrEMBL
other Location (Reliability: 4)
A0A3B0UNN9_9ZZZZ
222
0
25731
TrEMBL
other Location (Reliability: 2)
A0A0F4YTX1_TALEM
461
0
50903
TrEMBL
Mitochondrion (Reliability: 5)
A0A060TBC7_BLAAD
454
0
49618
TrEMBL
other Location (Reliability: 3)
A0A084GH64_PSEDA
448
0
48979
TrEMBL
other Location (Reliability: 5)
A0A0G2RK33_9PLEO
472
0
51551
TrEMBL
other Location (Reliability: 3)
A0A1W1HJ15_9DELT
444
0
49423
TrEMBL
-
A0A3B0TBF5_9ZZZZ
442
0
50220
TrEMBL
other Location (Reliability: 4)
A0A1W6VNB5_GEOTD
386
0
42520
TrEMBL
-
B9WEP0_CANDC
Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841)
444
0
49245
TrEMBL
other Location (Reliability: 5)
F2ICS7_FLUTR
Fluviicola taffensis (strain DSM 16823 / NCIMB 13979 / RW262)
445
0
50560
TrEMBL
-
A0A2H1E7S8_9FLAO
465
0
52845
TrEMBL
-
C0Q9S4_DESAH
Desulfobacterium autotrophicum (strain ATCC 43914 / DSM 3382 / HRM2)
395
0
43887
TrEMBL
-
A0A3B1BF66_9ZZZZ
207
0
22753
TrEMBL
other Location (Reliability: 3)
A0A3B0QRA3_9ZZZZ
149
0
16839
TrEMBL
other Location (Reliability: 1)
A0A3B1AEK9_9ZZZZ
251
0
27852
TrEMBL
other Location (Reliability: 1)
C5PG82_COCP7
Coccidioides posadasii (strain C735)
450
0
49471
TrEMBL
other Location (Reliability: 2)
G2PM06_MURRD
Muricauda ruestringensis (strain DSM 13258 / CIP 107369 / LMG 19739 / B1)
457
0
52295
TrEMBL
-
A0A3B0SGQ6_9ZZZZ
389
0
42158
TrEMBL
other Location (Reliability: 3)
A0A3B1CBV1_9ZZZZ
432
0
48681
TrEMBL
other Location (Reliability: 2)
A2QIZ4_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
448
0
49146
TrEMBL
other Location (Reliability: 5)
A0A2G9H4X7_9LAMI
411
0
44513
TrEMBL
Mitochondrion (Reliability: 3)
A0A0P8AAH9_9RHOB
208
0
23075
TrEMBL
-
T2KQ06_FORAG
Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901)
454
0
52127
TrEMBL
-
B8LW01_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
450
0
49607
TrEMBL
other Location (Reliability: 4)
A0A0F8DHK5_CERFI
450
0
48510
TrEMBL
other Location (Reliability: 5)
I3R7M9_HALMT
Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4)
412
0
44444
TrEMBL
-
S0G1D7_9DELT
392
0
42740
TrEMBL
-
C5A6R0_THEGJ
Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)
357
0
40117
TrEMBL
-
Q96TW2_PENCH
449
0
48752
TrEMBL
other Location (Reliability: 3)
E6X545_CELAD
Cellulophaga algicola (strain DSM 14237 / IC166 / ACAM 630)
457
0
52056
TrEMBL
-
F4L7G5_HALH1
Haliscomenobacter hydrossis (strain ATCC 27775 / DSM 1100 / LMG 10767 / O)
444
0
50209
TrEMBL
-
E4TQK6_MARTH
Marivirga tractuosa (strain ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB 1408 / VKM B-1430 / H-43)
446
0
50565
TrEMBL
-
G8TFI1_NIAKG
Niastella koreensis (strain DSM 17620 / KACC 11465 / NBRC 106392 / GR20-10)
504
0
56256
TrEMBL
-
W1QIX7_OGAPD
Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1)
445
0
48835
TrEMBL
other Location (Reliability: 3)
G0LAJ7_ZOBGA
Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij)
459
0
52506
TrEMBL
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
additional information
comparison of enzyme structures from Saccharomyces cerevisiae and Magnoporthe grisea
additional information
-
comparison of enzyme structures from Saccharomyces cerevisiae and Magnoporthe grisea
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of the apoenzyme crystal structure determined at 1.7 A resolution
apo form of enzyme. Protein consists of domain I, a variant of the Rossman fold and binding to NADPH, domain II with an alpha/beta structure and binding saccharopine, and domain III with all-helical fold involved in closing the active site of the enzyme once substrates are bound
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction of 3 Spe3-Lys9 mutants, with defects in the spe3-part, the lys9-part, or both, which are auxotrophic for lysine and spermidine, spermidine, and lysine, respectively, transcription levels and phenotype overview, the polyamine auxotrophy due to defect spe3 cannot be overcome by spermine addition, while the mutan with lys 9 defect grows slowly at 30°C with lysine addition, but dies upon lysine starvation, the mutant with defects in both gene parts is avirulent and lethal
additional information
-
construction of an enzyme-deficient mutant strain: disruption and inactivation of gene lys7 by double-recombination method leads to lysine auxotrophy and accumulation of piperideine-6-carboxylic acid, and with L-lysine as sole N-source and supplementation of DL-alpha-aminoadipic acid, also of pipecolic acid, transformation of the mutant strain with lys7 can restore enzyme activity
additional information
kinetic parameters of the mutants in the reaction direction of glutamate formation exhibit modest decreases. The pH-rate profiles obtained with all mutant enzymes decrease at low and high pH, suggesting acid and base catalytic groups are still present in all enzymes. Solvent kinetic deuterium isotope effects are all larger than those observed for wild-type enzyme
additional information
-
kinetic parameters of the mutants in the reaction direction of glutamate formation exhibit modest decreases. The pH-rate profiles obtained with all mutant enzymes decrease at low and high pH, suggesting acid and base catalytic groups are still present in all enzymes. Solvent kinetic deuterium isotope effects are all larger than those observed for wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene LYS9 is organized as a chimeric spermidine synthase-saccharopine dehydrogenase gene (SPE3-LYS9) encoding functional spermidine synthase, EC 2.5.1.16, and saccharopine dehydrogenase, DNA and amino acid sequence determination and analysis, expression of wild-type enzyme in Saccharomyces cerevisiae, the chimeric gene can complement a Saccharomyces cerevisiae lys9 mutant, but not a spe3 mutant
recombinant expression of wild-type and mutant enzymes in Saccharomyces cerevisiae strain LYS 9
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ye, Z.H.; Bhattacharjee, J.K.
Lysine biosynthesis pathway and biochemical blocks of lysine auxotrophs of Schizosaccharomyces pombe
J. Bacteriol.
170
5968-5970
1988
Schizosaccharomyces pombe
brenda
Naranjo, L.; Martin de Valmaseda, E.; Banuelos, O.; Lopez, P.; Riano, J.; Casqueiro, J.; Martin, J.F.
Conversion of pipecolic acid into lysine in Penicillium chrysogenum requires pipecolate oxidase and saccharopine reductase: characterization of the lys7 gene encoding saccharopine reductase
J. Bacteriol.
183
7165-7172
2001
Penicillium chrysogenum (Q96TW2), Penicillium chrysogenum
brenda
Mukhopadhyay, A.; Mungre, S.M.; Desmukh, D.R.
Comparison of lysine and tryptophan catabolizing enzymes in rat and bovine tissues
Experientia
46
874-876
1990
Bos taurus, Rattus norvegicus
brenda
Schmidt, H.; Bode, R.; Birnbaum, D.
Regulation of the lysine biosynthesis in Pichia guilliermondii
Antonie van Leeuwenhoek
56
337-347
1989
Meyerozyma guilliermondii
brenda
Broquist, H.P.
Aminoadipic semialdehyde-glutamate reductase
Methods Enzymol.
17B
121-124
1971
Saccharomyces cerevisiae
-
brenda
Jones, E.E.; Broquist, H.P.
Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis. 3. Aminoadipic semialdehyde-glutamate reductase
J. Biol. Chem.
241
3430-3434
1966
Saccharomyces cerevisiae
brenda
Storts, D.R.; Bhattacharjee, J.K.
Purification and properties of saccharopine dehydrogenase (glutamate forming) in the Saccharomyces cerevisiae lysine biosynthetic pathway
J. Bacteriol.
169
416-418
1987
Saccharomyces cerevisiae
brenda
Kinzel, J.J.; Bhattacharjee, J.K.
Role of pipecolic acid in the biosynthesis of lysine in Rhodotorula glutinis
J. Bacteriol.
138
410-417
1979
Rhodotorula glutinis
brenda
Johansson, E.; Steffens, J.J.; Emptage, M.; Lindqvist, Y.; Schneider, G.
Cloning, expression, purification and crystallization of saccharopine reductase from Magnaporthe grisea
Acta Crystallogr. Sect. D
56
662-664
2000
Pyricularia grisea
-
brenda
Naranjo, L.; Martin de Valmaseda, E.; Casqueiro, J.; Ullan, R.V.; Lamas-Maceiras, M.; Banuelos, O.; Martin, J.F.
Inactivation of the lys7 gene, encoding saccharopine reductase in Penicillium chrysogenum, leads to accumulation of the secondary metabolite precursors piperideine-6-carboxylic acid and pipecolic acid from alpha-aminoadipic acid
Appl. Environ. Microbiol.
70
1031-1039
2004
Penicillium chrysogenum
brenda
Kingsbury, J.M.; Yang, Z.; Ganous, T.M.; Cox, G.M.; McCusker, J.H.
Novel chimeric spermidine synthase-saccharopine dehydrogenase gene (SPE3-LYS9) in the human pathogen Cryptococcus neoformans
Eukaryot. Cell
3
752-763
2004
Cryptococcus neoformans (Q6RXX2)
brenda
Andi, B.; Cook, P.F.; West, A.H.
Crystal structure of the his-tagged saccharopine reductase from Saccharomyces cerevisiae at 1.7-A resolution
Cell Biochem. Biophys.
46
17-26
2006
Saccharomyces cerevisiae
brenda
Vashishtha, A.K.; West, A.H.; Cook, P.F.
Overall kinetic mechanism of saccharopine dehydrogenase (L-glutamate forming) from Saccharomyces cerevisiae
Biochemistry
47
5417-5423
2008
Saccharomyces cerevisiae
brenda
Vashishtha, A.K.; West, A.H.; Cook, P.F.
Chemical mechanism of saccharopine reductase from Saccharomyces cerevisiae
Biochemistry
48
5899-5907
2009
Saccharomyces cerevisiae
brenda
Almasi, J.; Bushnell, E.; Gauld, J.
A QM/MM-based computational investigation on the catalytic mechanism of saccharopine reductase
Molecules
16
8569-8589
2011
Pyricularia oryzae (Q9P4R4)
brenda
Vashishtha, A.K.; West, A.H.; Cook, P.F.
Probing the chemical mechanism of saccharopine reductase from Saccharomyces cerevisiae using site-directed mutagenesis
Arch. Biochem. Biophys.
584
98-106
2015
Saccharomyces cerevisiae (P38999), Saccharomyces cerevisiae
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.5.1.10)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Information
