We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
pyridoxamine-pyruvate aminotransferase, pyridoxamine-pyruvate transaminase,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
aminotransferase, pyridoxamine-pyruvate
-
-
-
PM-pyruvate transaminase
-
-
pyridoxamine-pyruvate aminotransferase
pyridoxamine-pyruvic transaminase
-
-
-
PPAT
-
pyridoxamine-pyruvate aminotransferase
-
-
-
pyridoxamine-pyruvate aminotransferase
-
pyridoxamine-pyruvate aminotransferase
pyridoxamine-2-oxoglutarate aminotransferase activity
pyridoxamine-pyruvate aminotransferase
-
-
pyridoxamine-pyruvate aminotransferase
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pyridoxamine + pyruvate = pyridoxal + L-alanine
pyridoxamine + pyruvate = pyridoxal + L-alanine
mechanism
-
pyridoxamine + pyruvate = pyridoxal + L-alanine
enzyme first binds pyridoxamine and then forms a Michaelis complex with the incoming pyruvate. The ketimine is formed through nucleophilic attack of the N-4' atom of pyridoxamine on the alpha-carbon atom of pyruvate, which is followed by the release of a water molecule. The stereospecific 1,3-prototropic shift between the ketimine and external aldimine via the quinonoid intermediate is accomplished through general base catalysis by Lys197. Pyridoxal and L-alanine are formed from the external aldimine and released from enzyme
pyridoxamine + pyruvate = pyridoxal + L-alanine
enzyme first binds pyridoxamine and then forms a Michaelis complex with the incoming pyruvate. The ketimine is formed through nucleophilic attack of the N-4' atom of pyridoxamine on the alpha-carbon atom of pyruvate, which is followed by the release of a water molecule. The stereospecific 1,3-prototropic shift between the ketimine and external aldimine via the quinonoid intermediate is accomplished through general base catalysis by Lys197. Pyridoxal and L-alanine are formed from the external aldimine and released from enzyme
-
pyridoxamine + pyruvate = pyridoxal + L-alanine
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
amino group transfer
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pyridoxamine:pyruvate aminotransferase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(S)-2-aminobutyrate + pyruvate
?
2-norpyridoxal + L-alanine
2-norpyridoxamine + pyruvate
-
-
-
r
3-hydroxypyridine-4-aldehyde + L-alanine
3-hydroxy-4-aminomethylpyridine + pyruvate
-
-
-
r
5-deoxypyridoxal + L-alanine
5-deoxypyridoxamine + pyruvate
omega-methylpyridoxal + L-alanine
omega-methylpyridoxamine + pyruvate
-
i.e. 3-hydroxy-5-hydroxymethyl-2-ethylpyridine-4-carboxaldehyde
-
r
pyridoxal + L-alanine
pyridoxamine + pyruvate
-
-
-
?
pyridoxamine + 2-oxobutyrate
?
pyridoxamine + 2-oxobutyrate
pyridoxal + (S)-2-aminobutyrate
poor substrate
-
r
pyridoxamine + 2-oxoglutarate
pyridoxal + L-glutamate
-
-
r
pyridoxamine + pyruvate
pyridoxal + L-alanine
pyridoxamine 5'-phosphate + pyruvate
pyridoxal 5'-phosphate + L-alanine
additional information
?
-
(S)-2-aminobutyrate + pyruvate
?
(S)-2-aminobutyrate is a poor substrate
-
?
(S)-2-aminobutyrate + pyruvate
?
-
(S)-2-aminobutyrate is a poor substrate
-
?
5-deoxypyridoxal + L-alanine
5-deoxypyridoxamine + pyruvate
-
-
-
r
5-deoxypyridoxal + L-alanine
5-deoxypyridoxamine + pyruvate
Soil bacterium
-
-
-
?
pyridoxamine + 2-oxobutyrate
?
-
-
?
pyridoxamine + 2-oxobutyrate
?
-
-
-
?
pyridoxamine + pyruvate
pyridoxal + L-alanine
-
-
?
pyridoxamine + pyruvate
pyridoxal + L-alanine
-
-
-
?
pyridoxamine + pyruvate
pyridoxal + L-alanine
-
-
r
pyridoxamine + pyruvate
pyridoxal + L-alanine
-
-
-
?
pyridoxamine + pyruvate
pyridoxal + L-alanine
-
-
?
pyridoxamine + pyruvate
pyridoxal + L-alanine
-
-
-
r
pyridoxamine + pyruvate
pyridoxal + L-alanine
-
-
-
?
pyridoxamine + pyruvate
pyridoxal + L-alanine
-
-
-
r
pyridoxamine + pyruvate
pyridoxal + L-alanine
-
-
-
r
pyridoxamine + pyruvate
pyridoxal + L-alanine
-
-
-
r
pyridoxamine + pyruvate
pyridoxal + L-alanine
-
oxaloacetate and several other keto acids tested cannot replace pyruvate as amino group acceptor
-
r
pyridoxamine + pyruvate
pyridoxal + L-alanine
Soil bacterium
-
-
-
r
pyridoxamine 5'-phosphate + pyruvate
pyridoxal 5'-phosphate + L-alanine
-
-
?
pyridoxamine 5'-phosphate + pyruvate
pyridoxal 5'-phosphate + L-alanine
-
-
?
additional information
?
-
-
the enzyme shows less than 0.5% of the activity of pyridoxamine towards pyridoxamine 5'-phosphate (3.3 mM) with pyruvate as the amino acceptor, the enzyme shows less than 0.5% of the activity of pyruvate towards 2-oxoglutarate, 3-hydroxypyruvate, indol-pyruvate, phenylpyruvate, 3-methyl-2-oxobutyrate and 4-hydroxyphenylpyruvate when they are used at 10 mM
-
?
additional information
?
-
the enzyme shows less than 0.5% of the activity of pyridoxamine towards pyridoxamine 5'-phosphate (3.3 mM) with pyruvate as the amino acceptor, the enzyme shows less than 0.5% of the activity of pyruvate towards 2-oxoglutarate, 3-hydroxypyruvate, indol-pyruvate, phenylpyruvate, 3-methyl-2-oxobutyrate and 4-hydroxyphenylpyruvate when they are used at 10 mM
-
?
additional information
?
-
-
the enzyme shows less than 0.5% of the activity of pyridoxamine towards pyridoxamine 5'-phosphate (3.3 mM) with pyruvate as the amino acceptor, the enzyme shows less than 0.5% of the activity of pyruvate towards 2-oxoglutarate, 3-hydroxypyruvate, indol-pyruvate, phenylpyruvate, 3-methyl-2-oxobutyrate and 4-hydroxyphenylpyruvate when they are used at 10 mM
-
?
additional information
?
-
-
no substrate: oxaloacetate, hydroxypyruvate and phenylpyruvate
-
?
additional information
?
-
-
not active with: 3-deoxypyridoxal, pyridine-4-aldehyde, O-methylpyridoxal, 4-nitrosalicylaldehyde
-
?
additional information
?
-
-
temperature-jump and stopped-flow kinetic investigation of the rate and mechanism of the reaction of 5'-deoxy-pyridoxal with the enzyme
-
?
additional information
?
-
-
determination of the active site stoichiometry and the pH dependence of the dissociation constant for 5'-deoxypyridoxal
-
?
additional information
?
-
-
enzyme is part of the degradative pathway for vitamin B6 compounds utilized by Pseudomonas sp. MA-1
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pyridoxamine + pyruvate
pyridoxal + L-alanine
additional information
?
-
-
enzyme is part of the degradative pathway for vitamin B6 compounds utilized by Pseudomonas sp. MA-1
-
-
?
pyridoxamine + pyruvate
pyridoxal + L-alanine
-
-
-
r
pyridoxamine + pyruvate
pyridoxal + L-alanine
-
-
-
r
pyridoxamine + pyruvate
pyridoxal + L-alanine
-
-
-
r
pyridoxamine + pyruvate
pyridoxal + L-alanine
-
oxaloacetate and several other keto acids tested cannot replace pyruvate as amino group acceptor
-
r
pyridoxamine + pyruvate
pyridoxal + L-alanine
Soil bacterium
-
-
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
the bulky side chain of Glu68 interferes with the binding of the phosphate moiety of pyridoxal 5'-phosphate and makes the enzyme specific to pyridoxal
additional information
-
pyridoxal 5'-phosphate is not required for activity
-
additional information
-
pyridoxal 5'-phosphate-independent enzyme
-
additional information
pyridoxal 5'-phosphate-independent enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3-Deoxypyridoxal
-
inhibits pyridoxamine formation from pyridoxal + alanine
4-Nitrosalicylaldehyde
-
inhibits pyridoxamine formation from pyridoxal + alanine
N-Methylpyridoxal
-
inhibits pyridoxamine formation from pyridoxal + alanine
O-Methylpyridoxal
-
inhibits pyridoxamine formation from pyridoxal + alanine
Pyridine-4-aldehyde
-
inhibits pyridoxamine formation from pyridoxal + alanine
additional information
-
hydroxylamine (10 mM), phenylhydrazine (1 mM) and sodium borohydride (1 mM) do not inactivate the enzyme
-
additional information
hydroxylamine (10 mM), phenylhydrazine (1 mM) and sodium borohydride (1 mM) do not inactivate the enzyme
-
additional information
-
not inhibitory: hydroxylamine, phenylhydrazine and sodium borohydride
-
additional information
-
phosphate is neither essential nor inhibitory
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
phosphate is neither essential nor inhibitory
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.59
2-norpyridoxal
-
pH 8.9, 25°C
0.16
2-Norpyridoxamine
-
pH 8.9, 25°C
8.8 - 110.3
2-oxoglutarate
0.89
3-hydroxypyridine-4-aldehyde
-
pH 8.9, 25°C
0.009
5-Deoxypyridoxal
-
pH 8.9, 25°C
0.014
5-Deoxypyridoxamine
-
pH 8.9, 25°C
1.3
omega-methylpyridoxal
-
pH 8.9, 25°C
3.4
pyridoxamine 5'-phosphate
mutant E68A, pH 9.0, 30°C
additional information
additional information
-
20
(S)-2-aminobutyrate
-
20
(S)-2-aminobutyrate
30°C, pH 9.0
7.1
2-oxobutyrate
-
7.1
2-oxobutyrate
30°C, pH 9.0
8.8
2-oxoglutarate
Y35H/V70R/F247C mutant protein, pH 9.0, 30°C
12.6
2-oxoglutarate
Y35H/V70K mutant protein, pH 9.0, 30°C
17.2
2-oxoglutarate
M2T/Y35H/V70K/E212G mutant protein, pH 9.0, 30°C
21.1
2-oxoglutarate
M2T/Y35H/V70K mutant protein, pH 9.0, 30°C
61.3
2-oxoglutarate
V70R/F247C mutant protein, pH 9.0, 30°C
77.3
2-oxoglutarate
M2T/V70K mutant protein, pH 9.0, 30°C
80.1
2-oxoglutarate
wild type protein, pH 9.0, 30°C
102.6
2-oxoglutarate
V70K mutant protein, pH 9.0, 30°C
106.8
2-oxoglutarate
M2T/V70K/E212G mutant protein, pH 9.0, 30°C
110.3
2-oxoglutarate
V70K/E212G mutant protein, pH 9.0, 30°C
0.58
L-alanine
-
with omega-methylpyridoxal, pH 8.9, 25°C
1.6
L-alanine
-
with pyridoxal, pH 8.9, 25°C
1.9
L-alanine
-
with 5-deoxypyridoxal, pH 8.9, 25°C
2.7
L-alanine
-
with 2-norpyridoxal, pH 8.9, 25°C
11
L-alanine
30°C, pH 9.0
64.5
L-alanine
-
with 3-hydroxypyridine-4-aldehyde, pH 8.9, 25°C
29.3
L-glutamate
Y35H/V70K mutant protein, pH 9.0, 30°C
42.4
L-glutamate
Y35H/V70R/F247C mutant protein, pH 9.0, 30°C
44.2
L-glutamate
M2T/Y35H/V70K mutant protein, pH 9.0, 30°C
51
L-glutamate
M2T/Y35H/V70K/E212G mutant protein, pH 9.0, 30°C
123.4
L-glutamate
wild type protein, pH 9.0, 30°C
133.5
L-glutamate
V70R/F247C mutant protein, pH 9.0, 30°C
142
L-glutamate
V70K mutant protein, pH 9.0, 30°C
0.012
pyridoxal
-
pH 8.9, 25°C
0.059
pyridoxal
30°C, pH 9.0
0.013
pyridoxamine
-
pH 8.9, 25°C
0.043
pyridoxamine
-
pH 8.5, 37°C
0.044
pyridoxamine
30°C, pH 9.0
0.044
pyridoxamine
wild-type, pH 9.0, 30°C
0.09
pyridoxamine
-
pH 8.5, 37°C
0.1
pyridoxamine
mutant R336A, pH 9.0, 30°C
0.35
pyridoxamine
-
with 3-hydroxy-4-aminomethylpyridine, pH 8.9, 25°C
1.3
pyridoxamine
mutant E68A, pH 9.0, 30°C
2.5
pyridoxamine
mutant E68G, pH 9.0, 30°C
0.1
pyruvate
-
pH 8.5, 37°C
0.31
pyruvate
-
pH 8.5, 37°C
0.34
pyruvate
30°C, pH 9.0
0.34
pyruvate
wild-type, pH 9.0, 30°C
0.35
pyruvate
-
with 3-hydroxy-4-aminomethylpyridine, pH 8.9, 25°C
0.4
pyruvate
-
with omega-methylpyridoxamine, pH 8.9, 25°C
0.42
pyruvate
-
with 5-deoxypyridoxamine, pH 8.9, 25°C
0.52
pyruvate
-
with 2-norpyridoxamine, pH 8.9, 25°C
6.9
pyruvate
mutant R336A, pH 9.0, 30°C
7.4
pyruvate
-
with 3-hydroxy-4-aminomethylpyridine, pH 8.9, 25°C
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
Soil bacterium
-
effect of pH on kinetic parameters
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.062 - 0.22
pyridoxamine 5'-phosphate
additional information
additional information
-
-
-
9
(S)-2-aminobutyrate
-
9
(S)-2-aminobutyrate
30°C, pH 9.0
24
2-oxobutyrate
-
24
2-oxobutyrate
30°C, pH 9.0
1.9
2-oxoglutarate
wild type protein, pH 9.0, 30°C
3.5
2-oxoglutarate
M2T/Y35H/V70K mutant protein, pH 9.0, 30°C
3.9
2-oxoglutarate
M2T/V70K mutant protein, pH 9.0, 30°C
4
2-oxoglutarate
M2T/Y35H/V70K/E212G mutant protein, pH 9.0, 30°C
4.1
2-oxoglutarate
V70K mutant protein, pH 9.0, 30°C
4.6
2-oxoglutarate
M2T/V70K/E212G mutant protein, pH 9.0, 30°C
4.6
2-oxoglutarate
V70K/E212G mutant protein, pH 9.0, 30°C
5.2
2-oxoglutarate
Y35H/V70K mutant protein, pH 9.0, 30°C
8.1
2-oxoglutarate
Y35H/V70R/F247C mutant protein, pH 9.0, 30°C
9.1
2-oxoglutarate
V70R/F247C mutant protein, pH 9.0, 30°C
41
L-alanine
-
41
L-alanine
30°C, pH 9.0
1.5
L-glutamate
wild type protein, pH 9.0, 30°C
2.7
L-glutamate
V70K mutant protein, pH 9.0, 30°C
2.9
L-glutamate
Y35H/V70K mutant protein, pH 9.0, 30°C
3
L-glutamate
M2T/Y35H/V70K/E212G mutant protein, pH 9.0, 30°C
3.1
L-glutamate
M2T/Y35H/V70K mutant protein, pH 9.0, 30°C
4.4
L-glutamate
V70R/F247C mutant protein, pH 9.0, 30°C
6.4
L-glutamate
Y35H/V70R/F247C mutant protein, pH 9.0, 30°C
41
pyridoxal
-
41
pyridoxal
30°C, pH 9.0
0.77
pyridoxamine
mutant E68G, pH 9.0, 30°C
0.78
pyridoxamine
mutant E68A, pH 9.0, 30°C
2 - 8
pyridoxamine
30°C, pH 9.0
2 - 8
pyridoxamine
mutant R336A, pH 9.0, 30°C
2 - 8
pyridoxamine
wild-type, pH 9.0, 30°C
0.062
pyridoxamine 5'-phosphate
mutant E68G, pH 9.0, 30°C
0.22
pyridoxamine 5'-phosphate
mutant E68A, pH 9.0, 30°C
29
pyruvate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.023 - 0.916
2-oxoglutarate
0.012 - 0.152
L-glutamate
0.023
2-oxoglutarate
wild type protein, pH 9.0, 30°C
0.04
2-oxoglutarate
V70K mutant protein, pH 9.0, 30°C
0.042
2-oxoglutarate
V70K/E212G mutant protein, pH 9.0, 30°C
0.043
2-oxoglutarate
M2T/V70K/E212G mutant protein, pH 9.0, 30°C
0.05
2-oxoglutarate
M2T/V70K mutant protein, pH 9.0, 30°C
0.148
2-oxoglutarate
V70R/F247C mutant protein, pH 9.0, 30°C
0.167
2-oxoglutarate
M2T/Y35H/V70K mutant protein, pH 9.0, 30°C
0.234
2-oxoglutarate
M2T/Y35H/V70K/E212G mutant protein, pH 9.0, 30°C
0.408
2-oxoglutarate
Y35H/V70K mutant protein, pH 9.0, 30°C
0.916
2-oxoglutarate
Y35H/V70R/F247C mutant protein, pH 9.0, 30°C
0.012
L-glutamate
wild type protein, pH 9.0, 30°C
0.019
L-glutamate
V70K mutant protein, pH 9.0, 30°C
0.033
L-glutamate
V70R/F247C mutant protein, pH 9.0, 30°C
0.058
L-glutamate
M2T/Y35H/V70K/E212G mutant protein, pH 9.0, 30°C
0.07
L-glutamate
M2T/Y35H/V70K mutant protein, pH 9.0, 30°C
0.1
L-glutamate
Y35H/V70K mutant protein, pH 9.0, 30°C
0.152
L-glutamate
Y35H/V70R/F247C mutant protein, pH 9.0, 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
9.5
estimated based on the Km and kcat values
8.5
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7 - 10
Soil bacterium
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
70
at pH 9, 100 mM borate/KOH buffer
70
in 100 mM borate/KOH buffer pH 9.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
30 - 80
30: 17% of maximal activity, 80°C: 3% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
Gram-negative bacillus isolate T2, 99.9% related to Ochrobactrum anthropi
-
-
brenda
-
-
-
brenda
Soil bacterium
-
-
-
brenda
-
-
-
brenda
-
SwissProt
brenda
-
-
-
brenda
-
SwissProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PPAT_RHILO
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
393
0
41590
Swiss-Prot
-
A0A644VNR5_9ZZZZ
394
0
41343
TrEMBL
Secretory Pathway (Reliability: 3 )
A0A387HJG1_9ACTN
376
0
38726
TrEMBL
-
A0A2S6R093_9PROT
392
0
41646
TrEMBL
-
A0A2P7ZA58_9ACTN
375
0
38467
TrEMBL
-
A0A645HL11_9ZZZZ
154
0
16653
TrEMBL
other Location (Reliability: 2 )
A0A6I1Z5A2_9ACTN
347
0
36138
TrEMBL
-
A0A509G0Y1_PAEPO
356
0
38192
TrEMBL
-
A0A140L8N7_9THEO
386
0
43007
TrEMBL
-
A0A385ZTI8_9ACTN
365
0
38158
TrEMBL
-
A0A162N3J3_9FIRM
383
0
43109
TrEMBL
-
A0A2S6X446_9ACTN
375
0
38645
TrEMBL
-
A0A1K2FXS3_9ACTN
373
0
38946
TrEMBL
-
A0A5P2YB35_RHISP
462
0
50034
TrEMBL
-
A0A1V2MQ89_9ACTN
368
0
38049
TrEMBL
-
A0A645DLQ6_9ZZZZ
254
0
27483
TrEMBL
other Location (Reliability: 1 )
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
32000
-
x * 32000, SDS-PAGE
41000
4 * 41000, SDS-PAGE
41000
4 * 41000, SDS-PAGE, gel filtration
41589
4 * 41589, calculated from amino acid sequence
41589
4 * 41589, calculated from sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
homotetramer
4 * 41000, SDS-PAGE
homotetramer
4 * 41589, calculated from amino acid sequence
homotetramer
4 * 41000, SDS-PAGE, gel filtration
homotetramer
-
4 * 41000, SDS-PAGE
homotetramer
-
4 * 41589, calculated from amino acid sequence
tetramer
4 * 41000, SDS-PAGE
tetramer
4 * 41589, calculated from sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
native enzyme, space group P43212, diffraction to 2.0 A resolution. Complexes with pyridoxamine, pyridoxal, and pyridoxyl-L-alanine at 1.7 A, 1.7 A, and 2.0 A resolution, respectively. Enzyme is a homotetramer and each subunit is composed of a large N-terminal domain, consisting of seven beta-sheets and eight alpha-helices, and a smaller C-terminal domain, consisting of three beta-sheets and four alpha-helices. The substrate pyridoxal is bound through an aldimine linkage to Lys197 in the active site. The carboxylate group of the substrate amino/keto acid is hydrogen-bonded to Arg336 and Arg345
addition of saturated ammonium sulfate solution to the concentrated protein solution until the first permanent turbidity appears, several days at 5°C
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
E68A
low pyridoxamine 5'-phosphate:pyruvate aminotransferase activity, decrease in activity towards pyridoxamine
E68G
low pyridoxamine 5'-phosphate:pyruvate aminotransferase activity, decrease in activity towards pyridoxamine
M2T/V70K
M2: surface residue
M2T/V70K/E212G
E212: surface residue
M2T/Y35H/V70K
Y35: active site residur
M2T/Y35H/V70K/E212G
E212: surface residue
R336A
significant decrease in affinity for pyruvate
V70K
active site residue, increase in reactivity toward 2-oxoglutarate
V70K/E212G
E212: surface residue
V70R
active site residue, elimination of activity
V70R/F247C
F247: hydrophobic core residue
Y35H/V70K
active site residues
Y35H/V70R/F247C
F247: hydrophobic core residue
C198A
-
shows activity of the wild type enzyme
E68A
-
low pyridoxamine 5'-phosphate:pyruvate aminotransferase activity, decrease in activity towards pyridoxamine
E68G
-
low pyridoxamine 5'-phosphate:pyruvate aminotransferase activity, decrease in activity towards pyridoxamine
K197L
-
shows no activity
R336A
-
significant decrease in affinity for pyruvate
C198A
enzyme shows the same specific activity as that of the wild type enzyme
C198A
shows activity of the wild type enzyme
K197L
mutant enzyme shows no activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
30 - 80
17% and 3% of the maximal activity is observed at 30°C and 80°C, respectively
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
loss of activity within 12 h at 25°C in sodium phosphate buffer, but is stable in potassium buffer under the same conditions
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
hydrophobic interaction chromatography, gel filtration
partial, QA52 column chromatography and butyl-Toyopearl column chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expressed in Escherichia coli BL21(DE3)
expressed in Escherichia coli strains JM109 and BL21(DE3)
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
analysis
determination method for individual natural vitamin B6 compounds. Compounds are specifically converted into 4-pyridoxolactone by pyridoxal 4-dehydrogenase and coupling reactions involving pyridoxine 4-oxidase, pyridoxal 4-dehydrogenase, or pyridoxamine-pyruvate aminotransferase and pyridoxal 4-dehydrogenase. Application of method for analysis of food samples
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Wada, H.; Snell, E.E.
Enzymatic transamination pf pyridoxamine. II. Crystalline pyridoxamine-pyruvate transaminase
J. Biol. Chem.
237
133-137
1962
Pseudomonas sp.
brenda
Ayling, J.E.; Snell, E.E.
Relation of structure to activity of pyridoxal analogs as substrates for pyridoxamine pyruvate transaminase
Biochemistry
7
1626-1636
1968
Pseudomonas sp.
brenda
Ford, J.B.
Effect of pH and temperature on kinetic parameters of pyridoxamine-pyruvate transaminase
J. Ala. Acad. Sci.
49
16-30
1978
Soil bacterium
-
brenda
Gilmer, P.J.; McIntire, W.S.; Kirsch, J.F.
Pyridoxamine-pyruvate transaminase. 1. Determination of the active site stoichiometry and the pH dependence of the dissociation constant for 5-deoxypyridoxal
Biochemistry
16
5241-5246
1977
Pseudomonas sp.
brenda
Gilmer, P.J.; Kirsch, J.F.
Pyridoxamine-pyruvate transaminase. 2. Temperature-jump and stopped-flow kinetic investigation of the rates and mechanism of the reaction of 5-deoxypyridoxal with the enzyme
Biochemistry
16
5246-5253
1977
Pseudomonas sp.
brenda
Yanee, T.; Suwanna, N.; Sineenat, S.
Vitamin B6 degradation by pyridoxamine-pyruvate transaminase and pyridoxine 4-oxidase from Ochrobactrum anthropi- and Enterobacter cloacae-like bacteria
Science Asia
31
307-311
2005
Ochrobactrum anthropi
-
brenda
Yoshikane, Y.; Yokochi, N.; Ohnishi, K.; Hayashi, H.; Yagi, T.
Molecular cloning, expression and characterization of pyridoxamine-pyruvate aminotransferase
Biochem. J.
396
499-507
2006
Mesorhizobium loti, Mesorhizobium loti (Q988B8), Mesorhizobium loti MAFF303099
brenda
Yoshikane, Y.; Yokochi, N.; Yamasaki, M.; Mizutani, K.; Ohnishi, K.; Mikami, B.; Hayashi, H.; Yagi, T.
Crystal structure of pyridoxamine-pyruvate aminotransferase from Mesorhizobium loti MAFF303099
J. Biol. Chem.
283
1120-1127
2008
Mesorhizobium loti (Q988B8), Mesorhizobium loti, Mesorhizobium loti MAFF303099 (Q988B8)
brenda
Nishimura, S.; Nagano, S.; A Crai, C.; Yokochi, N.; Yoshikane, Y.; Ge, F.; Yagi, T.
Determination of individual vitamin B(6) compounds based on enzymatic conversion to 4-pyridoxolactone
J. Nutr. Sci. Vitaminol.
54
18-24
2008
Mesorhizobium loti (Q988B8)
brenda
Yoshikane, Y.; Tamura, A.; Yokochi, N.; Ellouze, K.; Yamamura, E.; Mizunaga, H.; Fujimoto, N.; Sakamoto, K.; Sawa, Y.; Yagi, T.
Engineering Mesorhizobium loti pyridoxamine-pyruvate aminotransferase for production of pyridoxamine with L-glutamate as an amino donor
J. Mol. Catal. B
67
104-110
2010
Mesorhizobium loti (Q988B8)
-
brenda
Huang, S.; Zhang, J.; Wu, M.; Wu, Q.; Huang, L.
Enzymatic transamination of pyridoxamine in tobacco plants
Plant Sci.
212
55-59
2013
Nicotiana tabacum
brenda
Select items on the left to see more content.
html completed